Source 1primary paper2022Journal of Biological Chemistry
Toolkit/Aer PAS domain
Aer PAS domain
Also known as: Aer-PAS, Aer-PAS-GVV, PAS domain of Aer
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The Aer PAS domain is the FAD-binding sensory domain from the dimeric Escherichia coli aerotaxis receptor Aer. It monitors cellular respiration through a redox-sensitive flavin cofactor and is structurally characterized in the Aer-PAS-GVV variant at 2.4 Å resolution.
Usefulness & Problems
Why this is useful
This domain is useful as a defined redox-sensing module linked to cellular respiration in E. coli. The available redox measurement and crystal structure provide a basis for studying how PAS domains couple flavin chemistry to signaling, although direct tool-style applications are not described in the supplied evidence.
Problem solved
It addresses the biological problem of sensing cellular respiratory state through a protein-bound flavin cofactor. The evidence supports that the Aer PAS domain detects redox changes via FAD, but does not detail engineered use cases beyond this native sensing function.
Problem links
Need conditional control of signaling activity
DerivedThe Aer PAS domain is the FAD-binding sensory domain of the dimeric Escherichia coli aerotaxis receptor Aer. It monitors cellular respiration through a redox-sensitive FAD cofactor and transduces redox-dependent conformational changes to downstream signaling domains that regulate CheA kinase activity.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
conformational switchingconformational switchingConformational UncagingConformational UncagingHeterodimerizationHeterodimerizationredox sensingredox sensingsignal transduction to hamp and kinase control domainsTarget processes
signalingImplementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenoperating role: actuatoroperating role: sensorswitch architecture: multi componentswitch architecture: recruitmentswitch architecture: uncaging
The domain is from Escherichia coli Aer and binds an FAD cofactor for redox sensing. Structural information is available for the Aer-PAS-GVV variant, but the supplied evidence does not specify construct boundaries, expression conditions, or implementation guidance for engineered systems.
The supplied evidence is limited to one 2022 study and focuses on native biophysical characterization rather than broad functional deployment. Evidence for downstream signaling outputs, engineering performance, or validation in heterologous systems is not provided here.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
The Aer FADOX/FADASQ redox couple has a low formal potential of -289.6 ± 0.4 mV.
The Aer redox couple is remarkably low at -289.6 ± 0.4 mV.
formal potential -289.6 mVformal potential uncertainty 0.4 mV
The Aer FADOX/FADASQ redox couple has a low formal potential of -289.6 ± 0.4 mV.
The Aer redox couple is remarkably low at -289.6 ± 0.4 mV.
formal potential -289.6 mVformal potential uncertainty 0.4 mV
The Aer FADOX/FADASQ redox couple has a low formal potential of -289.6 ± 0.4 mV.
The Aer redox couple is remarkably low at -289.6 ± 0.4 mV.
formal potential -289.6 mVformal potential uncertainty 0.4 mV
The Aer FADOX/FADASQ redox couple has a low formal potential of -289.6 ± 0.4 mV.
The Aer redox couple is remarkably low at -289.6 ± 0.4 mV.
formal potential -289.6 mVformal potential uncertainty 0.4 mV
The Aer FADOX/FADASQ redox couple has a low formal potential of -289.6 ± 0.4 mV.
The Aer redox couple is remarkably low at -289.6 ± 0.4 mV.
formal potential -289.6 mVformal potential uncertainty 0.4 mV
The Aer FADOX/FADASQ redox couple has a low formal potential of -289.6 ± 0.4 mV.
The Aer redox couple is remarkably low at -289.6 ± 0.4 mV.
formal potential -289.6 mVformal potential uncertainty 0.4 mV
The Aer FADOX/FADASQ redox couple has a low formal potential of -289.6 ± 0.4 mV.
The Aer redox couple is remarkably low at -289.6 ± 0.4 mV.
formal potential -289.6 mVformal potential uncertainty 0.4 mV
The Aer FADOX/FADASQ redox couple has a low formal potential of -289.6 ± 0.4 mV.
The Aer redox couple is remarkably low at -289.6 ± 0.4 mV.
formal potential -289.6 mVformal potential uncertainty 0.4 mV
The Aer FADOX/FADASQ redox couple has a low formal potential of -289.6 ± 0.4 mV.
The Aer redox couple is remarkably low at -289.6 ± 0.4 mV.
formal potential -289.6 mVformal potential uncertainty 0.4 mV
The Aer FADOX/FADASQ redox couple has a low formal potential of -289.6 ± 0.4 mV.
The Aer redox couple is remarkably low at -289.6 ± 0.4 mV.
formal potential -289.6 mVformal potential uncertainty 0.4 mV
The Aer FADOX/FADASQ redox couple has a low formal potential of -289.6 ± 0.4 mV.
The Aer redox couple is remarkably low at -289.6 ± 0.4 mV.
formal potential -289.6 mVformal potential uncertainty 0.4 mV
The Aer FADOX/FADASQ redox couple has a low formal potential of -289.6 ± 0.4 mV.
The Aer redox couple is remarkably low at -289.6 ± 0.4 mV.
formal potential -289.6 mVformal potential uncertainty 0.4 mV
The Aer FADOX/FADASQ redox couple has a low formal potential of -289.6 ± 0.4 mV.
The Aer redox couple is remarkably low at -289.6 ± 0.4 mV.
formal potential -289.6 mVformal potential uncertainty 0.4 mV
The Aer FADOX/FADASQ redox couple has a low formal potential of -289.6 ± 0.4 mV.
The Aer redox couple is remarkably low at -289.6 ± 0.4 mV.
formal potential -289.6 mVformal potential uncertainty 0.4 mV
The Aer FADOX/FADASQ redox couple has a low formal potential of -289.6 ± 0.4 mV.
The Aer redox couple is remarkably low at -289.6 ± 0.4 mV.
formal potential -289.6 mVformal potential uncertainty 0.4 mV
The Aer FADOX/FADASQ redox couple has a low formal potential of -289.6 ± 0.4 mV.
The Aer redox couple is remarkably low at -289.6 ± 0.4 mV.
formal potential -289.6 mVformal potential uncertainty 0.4 mV
The Aer FADOX/FADASQ redox couple has a low formal potential of -289.6 ± 0.4 mV.
The Aer redox couple is remarkably low at -289.6 ± 0.4 mV.
formal potential -289.6 mVformal potential uncertainty 0.4 mV
The PAS domain of the Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive FAD cofactor.
The ... PAS domain of the dimeric Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive flavin adenine dinucleotide (FAD) cofactor.
The PAS domain of the Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive FAD cofactor.
The ... PAS domain of the dimeric Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive flavin adenine dinucleotide (FAD) cofactor.
The PAS domain of the Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive FAD cofactor.
The ... PAS domain of the dimeric Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive flavin adenine dinucleotide (FAD) cofactor.
The PAS domain of the Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive FAD cofactor.
The ... PAS domain of the dimeric Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive flavin adenine dinucleotide (FAD) cofactor.
The PAS domain of the Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive FAD cofactor.
The ... PAS domain of the dimeric Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive flavin adenine dinucleotide (FAD) cofactor.
The PAS domain of the Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive FAD cofactor.
The ... PAS domain of the dimeric Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive flavin adenine dinucleotide (FAD) cofactor.
The PAS domain of the Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive FAD cofactor.
The ... PAS domain of the dimeric Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive flavin adenine dinucleotide (FAD) cofactor.
The PAS domain of the Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive FAD cofactor.
The ... PAS domain of the dimeric Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive flavin adenine dinucleotide (FAD) cofactor.
The PAS domain of the Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive FAD cofactor.
The ... PAS domain of the dimeric Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive flavin adenine dinucleotide (FAD) cofactor.
The PAS domain of the Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive FAD cofactor.
The ... PAS domain of the dimeric Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive flavin adenine dinucleotide (FAD) cofactor.
The PAS domain of the Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive FAD cofactor.
The ... PAS domain of the dimeric Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive flavin adenine dinucleotide (FAD) cofactor.
The PAS domain of the Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive FAD cofactor.
The ... PAS domain of the dimeric Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive flavin adenine dinucleotide (FAD) cofactor.
The PAS domain of the Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive FAD cofactor.
The ... PAS domain of the dimeric Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive flavin adenine dinucleotide (FAD) cofactor.
The PAS domain of the Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive FAD cofactor.
The ... PAS domain of the dimeric Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive flavin adenine dinucleotide (FAD) cofactor.
The PAS domain of the Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive FAD cofactor.
The ... PAS domain of the dimeric Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive flavin adenine dinucleotide (FAD) cofactor.
The PAS domain of the Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive FAD cofactor.
The ... PAS domain of the dimeric Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive flavin adenine dinucleotide (FAD) cofactor.
The PAS domain of the Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive FAD cofactor.
The ... PAS domain of the dimeric Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive flavin adenine dinucleotide (FAD) cofactor.
Conformational shifts in the Aer PAS domain driven by the FADOX/FADASQ redox couple are transmitted through the HAMP and kinase control domains to regulate CheA kinase activity.
Conformational shifts in the PAS domain instigated by the oxidized FAD (FADOX)/FAD anionic semiquinone (FADASQ) redox couple traverse the HAMP and kinase control domains of the Aer dimer to regulate CheA kinase activity.
Conformational shifts in the Aer PAS domain driven by the FADOX/FADASQ redox couple are transmitted through the HAMP and kinase control domains to regulate CheA kinase activity.
Conformational shifts in the PAS domain instigated by the oxidized FAD (FADOX)/FAD anionic semiquinone (FADASQ) redox couple traverse the HAMP and kinase control domains of the Aer dimer to regulate CheA kinase activity.
Conformational shifts in the Aer PAS domain driven by the FADOX/FADASQ redox couple are transmitted through the HAMP and kinase control domains to regulate CheA kinase activity.
Conformational shifts in the PAS domain instigated by the oxidized FAD (FADOX)/FAD anionic semiquinone (FADASQ) redox couple traverse the HAMP and kinase control domains of the Aer dimer to regulate CheA kinase activity.
Conformational shifts in the Aer PAS domain driven by the FADOX/FADASQ redox couple are transmitted through the HAMP and kinase control domains to regulate CheA kinase activity.
Conformational shifts in the PAS domain instigated by the oxidized FAD (FADOX)/FAD anionic semiquinone (FADASQ) redox couple traverse the HAMP and kinase control domains of the Aer dimer to regulate CheA kinase activity.
Conformational shifts in the Aer PAS domain driven by the FADOX/FADASQ redox couple are transmitted through the HAMP and kinase control domains to regulate CheA kinase activity.
Conformational shifts in the PAS domain instigated by the oxidized FAD (FADOX)/FAD anionic semiquinone (FADASQ) redox couple traverse the HAMP and kinase control domains of the Aer dimer to regulate CheA kinase activity.
Conformational shifts in the Aer PAS domain driven by the FADOX/FADASQ redox couple are transmitted through the HAMP and kinase control domains to regulate CheA kinase activity.
Conformational shifts in the PAS domain instigated by the oxidized FAD (FADOX)/FAD anionic semiquinone (FADASQ) redox couple traverse the HAMP and kinase control domains of the Aer dimer to regulate CheA kinase activity.
Conformational shifts in the Aer PAS domain driven by the FADOX/FADASQ redox couple are transmitted through the HAMP and kinase control domains to regulate CheA kinase activity.
Conformational shifts in the PAS domain instigated by the oxidized FAD (FADOX)/FAD anionic semiquinone (FADASQ) redox couple traverse the HAMP and kinase control domains of the Aer dimer to regulate CheA kinase activity.
Conformational shifts in the Aer PAS domain driven by the FADOX/FADASQ redox couple are transmitted through the HAMP and kinase control domains to regulate CheA kinase activity.
Conformational shifts in the PAS domain instigated by the oxidized FAD (FADOX)/FAD anionic semiquinone (FADASQ) redox couple traverse the HAMP and kinase control domains of the Aer dimer to regulate CheA kinase activity.
Conformational shifts in the Aer PAS domain driven by the FADOX/FADASQ redox couple are transmitted through the HAMP and kinase control domains to regulate CheA kinase activity.
Conformational shifts in the PAS domain instigated by the oxidized FAD (FADOX)/FAD anionic semiquinone (FADASQ) redox couple traverse the HAMP and kinase control domains of the Aer dimer to regulate CheA kinase activity.
Conformational shifts in the Aer PAS domain driven by the FADOX/FADASQ redox couple are transmitted through the HAMP and kinase control domains to regulate CheA kinase activity.
Conformational shifts in the PAS domain instigated by the oxidized FAD (FADOX)/FAD anionic semiquinone (FADASQ) redox couple traverse the HAMP and kinase control domains of the Aer dimer to regulate CheA kinase activity.
Conformational shifts in the Aer PAS domain driven by the FADOX/FADASQ redox couple are transmitted through the HAMP and kinase control domains to regulate CheA kinase activity.
Conformational shifts in the PAS domain instigated by the oxidized FAD (FADOX)/FAD anionic semiquinone (FADASQ) redox couple traverse the HAMP and kinase control domains of the Aer dimer to regulate CheA kinase activity.
Conformational shifts in the Aer PAS domain driven by the FADOX/FADASQ redox couple are transmitted through the HAMP and kinase control domains to regulate CheA kinase activity.
Conformational shifts in the PAS domain instigated by the oxidized FAD (FADOX)/FAD anionic semiquinone (FADASQ) redox couple traverse the HAMP and kinase control domains of the Aer dimer to regulate CheA kinase activity.
Conformational shifts in the Aer PAS domain driven by the FADOX/FADASQ redox couple are transmitted through the HAMP and kinase control domains to regulate CheA kinase activity.
Conformational shifts in the PAS domain instigated by the oxidized FAD (FADOX)/FAD anionic semiquinone (FADASQ) redox couple traverse the HAMP and kinase control domains of the Aer dimer to regulate CheA kinase activity.
Conformational shifts in the Aer PAS domain driven by the FADOX/FADASQ redox couple are transmitted through the HAMP and kinase control domains to regulate CheA kinase activity.
Conformational shifts in the PAS domain instigated by the oxidized FAD (FADOX)/FAD anionic semiquinone (FADASQ) redox couple traverse the HAMP and kinase control domains of the Aer dimer to regulate CheA kinase activity.
Conformational shifts in the Aer PAS domain driven by the FADOX/FADASQ redox couple are transmitted through the HAMP and kinase control domains to regulate CheA kinase activity.
Conformational shifts in the PAS domain instigated by the oxidized FAD (FADOX)/FAD anionic semiquinone (FADASQ) redox couple traverse the HAMP and kinase control domains of the Aer dimer to regulate CheA kinase activity.
Conformational shifts in the Aer PAS domain driven by the FADOX/FADASQ redox couple are transmitted through the HAMP and kinase control domains to regulate CheA kinase activity.
Conformational shifts in the PAS domain instigated by the oxidized FAD (FADOX)/FAD anionic semiquinone (FADASQ) redox couple traverse the HAMP and kinase control domains of the Aer dimer to regulate CheA kinase activity.
Conformational shifts in the Aer PAS domain driven by the FADOX/FADASQ redox couple are transmitted through the HAMP and kinase control domains to regulate CheA kinase activity.
Conformational shifts in the PAS domain instigated by the oxidized FAD (FADOX)/FAD anionic semiquinone (FADASQ) redox couple traverse the HAMP and kinase control domains of the Aer dimer to regulate CheA kinase activity.
The authors propose a multistate model for Aer energy sensing based on the low potential of the Aer-PAS FADOX/FADASQ couple and the inability of Aer-PAS to bind fully reduced FAD hydroquinone.
In conclusion, we propose a model for Aer energy sensing based on the low potential of Aer-PAS-FADOX/FADASQ couple and the inability of Aer-PAS to bind to the fully reduced FAD hydroquinone.
The authors propose a multistate model for Aer energy sensing based on the low potential of the Aer-PAS FADOX/FADASQ couple and the inability of Aer-PAS to bind fully reduced FAD hydroquinone.
In conclusion, we propose a model for Aer energy sensing based on the low potential of Aer-PAS-FADOX/FADASQ couple and the inability of Aer-PAS to bind to the fully reduced FAD hydroquinone.
The authors propose a multistate model for Aer energy sensing based on the low potential of the Aer-PAS FADOX/FADASQ couple and the inability of Aer-PAS to bind fully reduced FAD hydroquinone.
In conclusion, we propose a model for Aer energy sensing based on the low potential of Aer-PAS-FADOX/FADASQ couple and the inability of Aer-PAS to bind to the fully reduced FAD hydroquinone.
The authors propose a multistate model for Aer energy sensing based on the low potential of the Aer-PAS FADOX/FADASQ couple and the inability of Aer-PAS to bind fully reduced FAD hydroquinone.
In conclusion, we propose a model for Aer energy sensing based on the low potential of Aer-PAS-FADOX/FADASQ couple and the inability of Aer-PAS to bind to the fully reduced FAD hydroquinone.
The authors propose a multistate model for Aer energy sensing based on the low potential of the Aer-PAS FADOX/FADASQ couple and the inability of Aer-PAS to bind fully reduced FAD hydroquinone.
In conclusion, we propose a model for Aer energy sensing based on the low potential of Aer-PAS-FADOX/FADASQ couple and the inability of Aer-PAS to bind to the fully reduced FAD hydroquinone.
The authors propose a multistate model for Aer energy sensing based on the low potential of the Aer-PAS FADOX/FADASQ couple and the inability of Aer-PAS to bind fully reduced FAD hydroquinone.
In conclusion, we propose a model for Aer energy sensing based on the low potential of Aer-PAS-FADOX/FADASQ couple and the inability of Aer-PAS to bind to the fully reduced FAD hydroquinone.
The authors propose a multistate model for Aer energy sensing based on the low potential of the Aer-PAS FADOX/FADASQ couple and the inability of Aer-PAS to bind fully reduced FAD hydroquinone.
In conclusion, we propose a model for Aer energy sensing based on the low potential of Aer-PAS-FADOX/FADASQ couple and the inability of Aer-PAS to bind to the fully reduced FAD hydroquinone.
The authors propose a multistate model for Aer energy sensing based on the low potential of the Aer-PAS FADOX/FADASQ couple and the inability of Aer-PAS to bind fully reduced FAD hydroquinone.
In conclusion, we propose a model for Aer energy sensing based on the low potential of Aer-PAS-FADOX/FADASQ couple and the inability of Aer-PAS to bind to the fully reduced FAD hydroquinone.
The authors propose a multistate model for Aer energy sensing based on the low potential of the Aer-PAS FADOX/FADASQ couple and the inability of Aer-PAS to bind fully reduced FAD hydroquinone.
In conclusion, we propose a model for Aer energy sensing based on the low potential of Aer-PAS-FADOX/FADASQ couple and the inability of Aer-PAS to bind to the fully reduced FAD hydroquinone.
The authors propose a multistate model for Aer energy sensing based on the low potential of the Aer-PAS FADOX/FADASQ couple and the inability of Aer-PAS to bind fully reduced FAD hydroquinone.
In conclusion, we propose a model for Aer energy sensing based on the low potential of Aer-PAS-FADOX/FADASQ couple and the inability of Aer-PAS to bind to the fully reduced FAD hydroquinone.
The authors propose a multistate model for Aer energy sensing based on the low potential of the Aer-PAS FADOX/FADASQ couple and the inability of Aer-PAS to bind fully reduced FAD hydroquinone.
In conclusion, we propose a model for Aer energy sensing based on the low potential of Aer-PAS-FADOX/FADASQ couple and the inability of Aer-PAS to bind to the fully reduced FAD hydroquinone.
The authors propose a multistate model for Aer energy sensing based on the low potential of the Aer-PAS FADOX/FADASQ couple and the inability of Aer-PAS to bind fully reduced FAD hydroquinone.
In conclusion, we propose a model for Aer energy sensing based on the low potential of Aer-PAS-FADOX/FADASQ couple and the inability of Aer-PAS to bind to the fully reduced FAD hydroquinone.
The authors propose a multistate model for Aer energy sensing based on the low potential of the Aer-PAS FADOX/FADASQ couple and the inability of Aer-PAS to bind fully reduced FAD hydroquinone.
In conclusion, we propose a model for Aer energy sensing based on the low potential of Aer-PAS-FADOX/FADASQ couple and the inability of Aer-PAS to bind to the fully reduced FAD hydroquinone.
The authors propose a multistate model for Aer energy sensing based on the low potential of the Aer-PAS FADOX/FADASQ couple and the inability of Aer-PAS to bind fully reduced FAD hydroquinone.
In conclusion, we propose a model for Aer energy sensing based on the low potential of Aer-PAS-FADOX/FADASQ couple and the inability of Aer-PAS to bind to the fully reduced FAD hydroquinone.
The authors propose a multistate model for Aer energy sensing based on the low potential of the Aer-PAS FADOX/FADASQ couple and the inability of Aer-PAS to bind fully reduced FAD hydroquinone.
In conclusion, we propose a model for Aer energy sensing based on the low potential of Aer-PAS-FADOX/FADASQ couple and the inability of Aer-PAS to bind to the fully reduced FAD hydroquinone.
The authors propose a multistate model for Aer energy sensing based on the low potential of the Aer-PAS FADOX/FADASQ couple and the inability of Aer-PAS to bind fully reduced FAD hydroquinone.
In conclusion, we propose a model for Aer energy sensing based on the low potential of Aer-PAS-FADOX/FADASQ couple and the inability of Aer-PAS to bind to the fully reduced FAD hydroquinone.
The authors propose a multistate model for Aer energy sensing based on the low potential of the Aer-PAS FADOX/FADASQ couple and the inability of Aer-PAS to bind fully reduced FAD hydroquinone.
In conclusion, we propose a model for Aer energy sensing based on the low potential of Aer-PAS-FADOX/FADASQ couple and the inability of Aer-PAS to bind to the fully reduced FAD hydroquinone.
Aer-PAS-GVV was solved at 2.4 Å resolution and its PAS fold contains features associated with FAD-based redox sensing, including contacts involving Arg115, His53, and Asn85.
We solved the 2.4 Å resolution crystal structure of this variant, Aer-PAS-GVV, and revealed a PAS fold that contains distinct features associated with FAD-based redox sensing
crystal structure resolution 2.4 Å
Aer-PAS-GVV was solved at 2.4 Å resolution and its PAS fold contains features associated with FAD-based redox sensing, including contacts involving Arg115, His53, and Asn85.
We solved the 2.4 Å resolution crystal structure of this variant, Aer-PAS-GVV, and revealed a PAS fold that contains distinct features associated with FAD-based redox sensing
crystal structure resolution 2.4 Å
Aer-PAS-GVV was solved at 2.4 Å resolution and its PAS fold contains features associated with FAD-based redox sensing, including contacts involving Arg115, His53, and Asn85.
We solved the 2.4 Å resolution crystal structure of this variant, Aer-PAS-GVV, and revealed a PAS fold that contains distinct features associated with FAD-based redox sensing
crystal structure resolution 2.4 Å
Aer-PAS-GVV was solved at 2.4 Å resolution and its PAS fold contains features associated with FAD-based redox sensing, including contacts involving Arg115, His53, and Asn85.
We solved the 2.4 Å resolution crystal structure of this variant, Aer-PAS-GVV, and revealed a PAS fold that contains distinct features associated with FAD-based redox sensing
crystal structure resolution 2.4 Å
Aer-PAS-GVV was solved at 2.4 Å resolution and its PAS fold contains features associated with FAD-based redox sensing, including contacts involving Arg115, His53, and Asn85.
We solved the 2.4 Å resolution crystal structure of this variant, Aer-PAS-GVV, and revealed a PAS fold that contains distinct features associated with FAD-based redox sensing
crystal structure resolution 2.4 Å
Aer-PAS-GVV was solved at 2.4 Å resolution and its PAS fold contains features associated with FAD-based redox sensing, including contacts involving Arg115, His53, and Asn85.
We solved the 2.4 Å resolution crystal structure of this variant, Aer-PAS-GVV, and revealed a PAS fold that contains distinct features associated with FAD-based redox sensing
crystal structure resolution 2.4 Å
Aer-PAS-GVV was solved at 2.4 Å resolution and its PAS fold contains features associated with FAD-based redox sensing, including contacts involving Arg115, His53, and Asn85.
We solved the 2.4 Å resolution crystal structure of this variant, Aer-PAS-GVV, and revealed a PAS fold that contains distinct features associated with FAD-based redox sensing
crystal structure resolution 2.4 Å
Aer-PAS-GVV was solved at 2.4 Å resolution and its PAS fold contains features associated with FAD-based redox sensing, including contacts involving Arg115, His53, and Asn85.
We solved the 2.4 Å resolution crystal structure of this variant, Aer-PAS-GVV, and revealed a PAS fold that contains distinct features associated with FAD-based redox sensing
crystal structure resolution 2.4 Å
Aer-PAS-GVV was solved at 2.4 Å resolution and its PAS fold contains features associated with FAD-based redox sensing, including contacts involving Arg115, His53, and Asn85.
We solved the 2.4 Å resolution crystal structure of this variant, Aer-PAS-GVV, and revealed a PAS fold that contains distinct features associated with FAD-based redox sensing
crystal structure resolution 2.4 Å
Aer-PAS-GVV was solved at 2.4 Å resolution and its PAS fold contains features associated with FAD-based redox sensing, including contacts involving Arg115, His53, and Asn85.
We solved the 2.4 Å resolution crystal structure of this variant, Aer-PAS-GVV, and revealed a PAS fold that contains distinct features associated with FAD-based redox sensing
crystal structure resolution 2.4 Å
Aer-PAS-GVV was solved at 2.4 Å resolution and its PAS fold contains features associated with FAD-based redox sensing, including contacts involving Arg115, His53, and Asn85.
We solved the 2.4 Å resolution crystal structure of this variant, Aer-PAS-GVV, and revealed a PAS fold that contains distinct features associated with FAD-based redox sensing
crystal structure resolution 2.4 Å
Aer-PAS-GVV was solved at 2.4 Å resolution and its PAS fold contains features associated with FAD-based redox sensing, including contacts involving Arg115, His53, and Asn85.
We solved the 2.4 Å resolution crystal structure of this variant, Aer-PAS-GVV, and revealed a PAS fold that contains distinct features associated with FAD-based redox sensing
crystal structure resolution 2.4 Å
Aer-PAS-GVV was solved at 2.4 Å resolution and its PAS fold contains features associated with FAD-based redox sensing, including contacts involving Arg115, His53, and Asn85.
We solved the 2.4 Å resolution crystal structure of this variant, Aer-PAS-GVV, and revealed a PAS fold that contains distinct features associated with FAD-based redox sensing
crystal structure resolution 2.4 Å
Aer-PAS-GVV was solved at 2.4 Å resolution and its PAS fold contains features associated with FAD-based redox sensing, including contacts involving Arg115, His53, and Asn85.
We solved the 2.4 Å resolution crystal structure of this variant, Aer-PAS-GVV, and revealed a PAS fold that contains distinct features associated with FAD-based redox sensing
crystal structure resolution 2.4 Å
Aer-PAS-GVV was solved at 2.4 Å resolution and its PAS fold contains features associated with FAD-based redox sensing, including contacts involving Arg115, His53, and Asn85.
We solved the 2.4 Å resolution crystal structure of this variant, Aer-PAS-GVV, and revealed a PAS fold that contains distinct features associated with FAD-based redox sensing
crystal structure resolution 2.4 Å
Aer-PAS-GVV was solved at 2.4 Å resolution and its PAS fold contains features associated with FAD-based redox sensing, including contacts involving Arg115, His53, and Asn85.
We solved the 2.4 Å resolution crystal structure of this variant, Aer-PAS-GVV, and revealed a PAS fold that contains distinct features associated with FAD-based redox sensing
crystal structure resolution 2.4 Å
Aer-PAS-GVV was solved at 2.4 Å resolution and its PAS fold contains features associated with FAD-based redox sensing, including contacts involving Arg115, His53, and Asn85.
We solved the 2.4 Å resolution crystal structure of this variant, Aer-PAS-GVV, and revealed a PAS fold that contains distinct features associated with FAD-based redox sensing
crystal structure resolution 2.4 Å
Approval Evidence
1 source5 linked approval claimsfirst-pass slug aer-pas-domain
The PAS domain of the dimeric Escherichia coli aerotaxis receptor Aer ... We solved the 2.4 Å resolution crystal structure of this variant, Aer-PAS-GVV
Source:
biophysical propertysupports
The Aer FADOX/FADASQ redox couple has a low formal potential of -289.6 ± 0.4 mV.
The Aer redox couple is remarkably low at -289.6 ± 0.4 mV.
Source:
functionsupports
The PAS domain of the Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive FAD cofactor.
The ... PAS domain of the dimeric Escherichia coli aerotaxis receptor Aer monitors cellular respiration through a redox-sensitive flavin adenine dinucleotide (FAD) cofactor.
Source:
mechanismsupports
Conformational shifts in the Aer PAS domain driven by the FADOX/FADASQ redox couple are transmitted through the HAMP and kinase control domains to regulate CheA kinase activity.
Conformational shifts in the PAS domain instigated by the oxidized FAD (FADOX)/FAD anionic semiquinone (FADASQ) redox couple traverse the HAMP and kinase control domains of the Aer dimer to regulate CheA kinase activity.
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mechanistic modelsupports
The authors propose a multistate model for Aer energy sensing based on the low potential of the Aer-PAS FADOX/FADASQ couple and the inability of Aer-PAS to bind fully reduced FAD hydroquinone.
In conclusion, we propose a model for Aer energy sensing based on the low potential of Aer-PAS-FADOX/FADASQ couple and the inability of Aer-PAS to bind to the fully reduced FAD hydroquinone.
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structural observationsupports
Aer-PAS-GVV was solved at 2.4 Å resolution and its PAS fold contains features associated with FAD-based redox sensing, including contacts involving Arg115, His53, and Asn85.
We solved the 2.4 Å resolution crystal structure of this variant, Aer-PAS-GVV, and revealed a PAS fold that contains distinct features associated with FAD-based redox sensing
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Comparisons
Source-backed strengths
The domain has a quantitatively measured FADox/FADasq redox couple with a low formal potential of -289.6 ± 0.4 mV, providing a precise biophysical benchmark. It is also supported by a 2.4 Å crystal structure of the Aer-PAS-GVV variant, which strengthens mechanistic interpretation of its redox-sensing state behavior.
Compared with Arabidopsis thaliana cryptochrome 2
Aer PAS domain and Arabidopsis thaliana cryptochrome 2 address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: heterodimerization
Relative tradeoffs: appears more independently replicated.
Compared with EL346
Aer PAS domain and EL346 address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: heterodimerization
Strengths here: looks easier to implement in practice.
Compared with light-oxygen-voltage sensing (LOV) domain
Aer PAS domain and light-oxygen-voltage sensing (LOV) domain address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: heterodimerization
Strengths here: looks easier to implement in practice.
Ranked Citations
- 1.