Source 1primary paper2004Journal of Biological Chemistry
Toolkit/heme PAS domain of Ec DOS
heme PAS domain of Ec DOS
Also known as: bacterial heme PAS sensor, Ec DOS heme PAS domain
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The heme PAS domain of Escherichia coli direct oxygen sensor (Ec DOS) is a bacterial heme-binding sensor domain structurally characterized in inactive Fe(3+) and active Fe(2+) states. It acts as a redox-responsive molecular switch in which changes in heme coordination are coupled to conformational rearrangements within the PAS domain.
Usefulness & Problems
Why this is useful
This domain is useful as a structurally defined model for understanding how heme redox state can be converted into protein conformational output. The available crystal structures link specific coordination changes at the heme iron to loop rigidification, altered hydrogen bonding, and subunit rotation.
Problem solved
It helps address the problem of how a heme-based sensor domain distinguishes inactive oxidized and active reduced states at the structural level. The reported structures provide a mechanistic framework connecting Fe(3+)/Fe(2+) state changes to local ligand switching and larger-scale domain rearrangements.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
conformational switchingconformational switchingheme ligand switchingheme ligand switchingHeterodimerizationredox-controlled switchingredox-controlled switchingsubunit rotationsubunit rotationTechniques
Structural CharacterizationTarget processes
No target processes tagged yet.
Input: Chemical
Implementation 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: recruitment
The domain is a heme-binding PAS sensor from E. coli DOS, and its characterized states depend on the oxidation state of the heme iron. The evidence indicates His-77/water ligation in the Fe(3+) state and Met-95 involvement after reduction, but no additional construct design, expression, or delivery details are provided in the supplied material.
The supplied evidence is limited to a single structural study and does not document broader functional validation, engineering use, or performance in heterologous systems. Evidence for practical deployment as a modular tool, input specificity beyond redox state, and generalizability across contexts is not provided here.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
The heme PAS domain of Ec DOS was structurally characterized in inactive Fe(3+) and active Fe(2+) forms.
Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms at 1.32 and 1.9 A resolution, respectively.
crystal structure resolution Fe(2+) form 1.9 Acrystal structure resolution Fe(3+) form 1.32 A
The heme PAS domain of Ec DOS was structurally characterized in inactive Fe(3+) and active Fe(2+) forms.
Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms at 1.32 and 1.9 A resolution, respectively.
crystal structure resolution Fe(2+) form 1.9 Acrystal structure resolution Fe(3+) form 1.32 A
The heme PAS domain of Ec DOS was structurally characterized in inactive Fe(3+) and active Fe(2+) forms.
Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms at 1.32 and 1.9 A resolution, respectively.
crystal structure resolution Fe(2+) form 1.9 Acrystal structure resolution Fe(3+) form 1.32 A
The heme PAS domain of Ec DOS was structurally characterized in inactive Fe(3+) and active Fe(2+) forms.
Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms at 1.32 and 1.9 A resolution, respectively.
crystal structure resolution Fe(2+) form 1.9 Acrystal structure resolution Fe(3+) form 1.32 A
The heme PAS domain of Ec DOS was structurally characterized in inactive Fe(3+) and active Fe(2+) forms.
Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms at 1.32 and 1.9 A resolution, respectively.
crystal structure resolution Fe(2+) form 1.9 Acrystal structure resolution Fe(3+) form 1.32 A
The heme PAS domain of Ec DOS was structurally characterized in inactive Fe(3+) and active Fe(2+) forms.
Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms at 1.32 and 1.9 A resolution, respectively.
crystal structure resolution Fe(2+) form 1.9 Acrystal structure resolution Fe(3+) form 1.32 A
The heme PAS domain of Ec DOS was structurally characterized in inactive Fe(3+) and active Fe(2+) forms.
Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms at 1.32 and 1.9 A resolution, respectively.
crystal structure resolution Fe(2+) form 1.9 Acrystal structure resolution Fe(3+) form 1.32 A
The heme PAS domain of Ec DOS was structurally characterized in inactive Fe(3+) and active Fe(2+) forms.
Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms at 1.32 and 1.9 A resolution, respectively.
crystal structure resolution Fe(2+) form 1.9 Acrystal structure resolution Fe(3+) form 1.32 A
The heme PAS domain of Ec DOS was structurally characterized in inactive Fe(3+) and active Fe(2+) forms.
Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms at 1.32 and 1.9 A resolution, respectively.
crystal structure resolution Fe(2+) form 1.9 Acrystal structure resolution Fe(3+) form 1.32 A
The heme PAS domain of Ec DOS was structurally characterized in inactive Fe(3+) and active Fe(2+) forms.
Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms at 1.32 and 1.9 A resolution, respectively.
crystal structure resolution Fe(2+) form 1.9 Acrystal structure resolution Fe(3+) form 1.32 A
The heme PAS domain of Ec DOS was structurally characterized in inactive Fe(3+) and active Fe(2+) forms.
Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms at 1.32 and 1.9 A resolution, respectively.
crystal structure resolution Fe(2+) form 1.9 Acrystal structure resolution Fe(3+) form 1.32 A
The heme PAS domain of Ec DOS was structurally characterized in inactive Fe(3+) and active Fe(2+) forms.
Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms at 1.32 and 1.9 A resolution, respectively.
crystal structure resolution Fe(2+) form 1.9 Acrystal structure resolution Fe(3+) form 1.32 A
The heme PAS domain of Ec DOS was structurally characterized in inactive Fe(3+) and active Fe(2+) forms.
Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms at 1.32 and 1.9 A resolution, respectively.
crystal structure resolution Fe(2+) form 1.9 Acrystal structure resolution Fe(3+) form 1.32 A
The heme PAS domain of Ec DOS was structurally characterized in inactive Fe(3+) and active Fe(2+) forms.
Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms at 1.32 and 1.9 A resolution, respectively.
crystal structure resolution Fe(2+) form 1.9 Acrystal structure resolution Fe(3+) form 1.32 A
The heme PAS domain of Ec DOS was structurally characterized in inactive Fe(3+) and active Fe(2+) forms.
Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms at 1.32 and 1.9 A resolution, respectively.
crystal structure resolution Fe(2+) form 1.9 Acrystal structure resolution Fe(3+) form 1.32 A
The heme PAS domain of Ec DOS was structurally characterized in inactive Fe(3+) and active Fe(2+) forms.
Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms at 1.32 and 1.9 A resolution, respectively.
crystal structure resolution Fe(2+) form 1.9 Acrystal structure resolution Fe(3+) form 1.32 A
The heme PAS domain of Ec DOS was structurally characterized in inactive Fe(3+) and active Fe(2+) forms.
Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms at 1.32 and 1.9 A resolution, respectively.
crystal structure resolution Fe(2+) form 1.9 Acrystal structure resolution Fe(3+) form 1.32 A
Reduction of heme iron in the Ec DOS heme PAS domain is accompanied by ligand switching from water to Met-95, FG loop rigidification, altered hydrogen bonding, and subunit rotation.
Heme iron reduction is accompanied by heme-ligand switching from the water molecule to a side chain of Met-95 from the FG loop. Concomitantly, the flexible FG loop is significantly rigidified, along with a change in the hydrogen bonding pattern and rotation of subunits relative to each other.
Reduction of heme iron in the Ec DOS heme PAS domain is accompanied by ligand switching from water to Met-95, FG loop rigidification, altered hydrogen bonding, and subunit rotation.
Heme iron reduction is accompanied by heme-ligand switching from the water molecule to a side chain of Met-95 from the FG loop. Concomitantly, the flexible FG loop is significantly rigidified, along with a change in the hydrogen bonding pattern and rotation of subunits relative to each other.
Reduction of heme iron in the Ec DOS heme PAS domain is accompanied by ligand switching from water to Met-95, FG loop rigidification, altered hydrogen bonding, and subunit rotation.
Heme iron reduction is accompanied by heme-ligand switching from the water molecule to a side chain of Met-95 from the FG loop. Concomitantly, the flexible FG loop is significantly rigidified, along with a change in the hydrogen bonding pattern and rotation of subunits relative to each other.
Reduction of heme iron in the Ec DOS heme PAS domain is accompanied by ligand switching from water to Met-95, FG loop rigidification, altered hydrogen bonding, and subunit rotation.
Heme iron reduction is accompanied by heme-ligand switching from the water molecule to a side chain of Met-95 from the FG loop. Concomitantly, the flexible FG loop is significantly rigidified, along with a change in the hydrogen bonding pattern and rotation of subunits relative to each other.
Reduction of heme iron in the Ec DOS heme PAS domain is accompanied by ligand switching from water to Met-95, FG loop rigidification, altered hydrogen bonding, and subunit rotation.
Heme iron reduction is accompanied by heme-ligand switching from the water molecule to a side chain of Met-95 from the FG loop. Concomitantly, the flexible FG loop is significantly rigidified, along with a change in the hydrogen bonding pattern and rotation of subunits relative to each other.
Reduction of heme iron in the Ec DOS heme PAS domain is accompanied by ligand switching from water to Met-95, FG loop rigidification, altered hydrogen bonding, and subunit rotation.
Heme iron reduction is accompanied by heme-ligand switching from the water molecule to a side chain of Met-95 from the FG loop. Concomitantly, the flexible FG loop is significantly rigidified, along with a change in the hydrogen bonding pattern and rotation of subunits relative to each other.
Reduction of heme iron in the Ec DOS heme PAS domain is accompanied by ligand switching from water to Met-95, FG loop rigidification, altered hydrogen bonding, and subunit rotation.
Heme iron reduction is accompanied by heme-ligand switching from the water molecule to a side chain of Met-95 from the FG loop. Concomitantly, the flexible FG loop is significantly rigidified, along with a change in the hydrogen bonding pattern and rotation of subunits relative to each other.
Reduction of heme iron in the Ec DOS heme PAS domain is accompanied by ligand switching from water to Met-95, FG loop rigidification, altered hydrogen bonding, and subunit rotation.
Heme iron reduction is accompanied by heme-ligand switching from the water molecule to a side chain of Met-95 from the FG loop. Concomitantly, the flexible FG loop is significantly rigidified, along with a change in the hydrogen bonding pattern and rotation of subunits relative to each other.
Reduction of heme iron in the Ec DOS heme PAS domain is accompanied by ligand switching from water to Met-95, FG loop rigidification, altered hydrogen bonding, and subunit rotation.
Heme iron reduction is accompanied by heme-ligand switching from the water molecule to a side chain of Met-95 from the FG loop. Concomitantly, the flexible FG loop is significantly rigidified, along with a change in the hydrogen bonding pattern and rotation of subunits relative to each other.
Reduction of heme iron in the Ec DOS heme PAS domain is accompanied by ligand switching from water to Met-95, FG loop rigidification, altered hydrogen bonding, and subunit rotation.
Heme iron reduction is accompanied by heme-ligand switching from the water molecule to a side chain of Met-95 from the FG loop. Concomitantly, the flexible FG loop is significantly rigidified, along with a change in the hydrogen bonding pattern and rotation of subunits relative to each other.
Reduction of heme iron in the Ec DOS heme PAS domain is accompanied by ligand switching from water to Met-95, FG loop rigidification, altered hydrogen bonding, and subunit rotation.
Heme iron reduction is accompanied by heme-ligand switching from the water molecule to a side chain of Met-95 from the FG loop. Concomitantly, the flexible FG loop is significantly rigidified, along with a change in the hydrogen bonding pattern and rotation of subunits relative to each other.
Reduction of heme iron in the Ec DOS heme PAS domain is accompanied by ligand switching from water to Met-95, FG loop rigidification, altered hydrogen bonding, and subunit rotation.
Heme iron reduction is accompanied by heme-ligand switching from the water molecule to a side chain of Met-95 from the FG loop. Concomitantly, the flexible FG loop is significantly rigidified, along with a change in the hydrogen bonding pattern and rotation of subunits relative to each other.
Reduction of heme iron in the Ec DOS heme PAS domain is accompanied by ligand switching from water to Met-95, FG loop rigidification, altered hydrogen bonding, and subunit rotation.
Heme iron reduction is accompanied by heme-ligand switching from the water molecule to a side chain of Met-95 from the FG loop. Concomitantly, the flexible FG loop is significantly rigidified, along with a change in the hydrogen bonding pattern and rotation of subunits relative to each other.
Reduction of heme iron in the Ec DOS heme PAS domain is accompanied by ligand switching from water to Met-95, FG loop rigidification, altered hydrogen bonding, and subunit rotation.
Heme iron reduction is accompanied by heme-ligand switching from the water molecule to a side chain of Met-95 from the FG loop. Concomitantly, the flexible FG loop is significantly rigidified, along with a change in the hydrogen bonding pattern and rotation of subunits relative to each other.
Reduction of heme iron in the Ec DOS heme PAS domain is accompanied by ligand switching from water to Met-95, FG loop rigidification, altered hydrogen bonding, and subunit rotation.
Heme iron reduction is accompanied by heme-ligand switching from the water molecule to a side chain of Met-95 from the FG loop. Concomitantly, the flexible FG loop is significantly rigidified, along with a change in the hydrogen bonding pattern and rotation of subunits relative to each other.
Reduction of heme iron in the Ec DOS heme PAS domain is accompanied by ligand switching from water to Met-95, FG loop rigidification, altered hydrogen bonding, and subunit rotation.
Heme iron reduction is accompanied by heme-ligand switching from the water molecule to a side chain of Met-95 from the FG loop. Concomitantly, the flexible FG loop is significantly rigidified, along with a change in the hydrogen bonding pattern and rotation of subunits relative to each other.
Reduction of heme iron in the Ec DOS heme PAS domain is accompanied by ligand switching from water to Met-95, FG loop rigidification, altered hydrogen bonding, and subunit rotation.
Heme iron reduction is accompanied by heme-ligand switching from the water molecule to a side chain of Met-95 from the FG loop. Concomitantly, the flexible FG loop is significantly rigidified, along with a change in the hydrogen bonding pattern and rotation of subunits relative to each other.
In the Fe(3+) form of the Ec DOS heme PAS domain, the heme iron is ligated by His-77 and a water molecule.
In the Fe(3+) form, the heme iron is ligated to a His-77 side chain and a water molecule.
In the Fe(3+) form of the Ec DOS heme PAS domain, the heme iron is ligated by His-77 and a water molecule.
In the Fe(3+) form, the heme iron is ligated to a His-77 side chain and a water molecule.
In the Fe(3+) form of the Ec DOS heme PAS domain, the heme iron is ligated by His-77 and a water molecule.
In the Fe(3+) form, the heme iron is ligated to a His-77 side chain and a water molecule.
In the Fe(3+) form of the Ec DOS heme PAS domain, the heme iron is ligated by His-77 and a water molecule.
In the Fe(3+) form, the heme iron is ligated to a His-77 side chain and a water molecule.
In the Fe(3+) form of the Ec DOS heme PAS domain, the heme iron is ligated by His-77 and a water molecule.
In the Fe(3+) form, the heme iron is ligated to a His-77 side chain and a water molecule.
In the Fe(3+) form of the Ec DOS heme PAS domain, the heme iron is ligated by His-77 and a water molecule.
In the Fe(3+) form, the heme iron is ligated to a His-77 side chain and a water molecule.
In the Fe(3+) form of the Ec DOS heme PAS domain, the heme iron is ligated by His-77 and a water molecule.
In the Fe(3+) form, the heme iron is ligated to a His-77 side chain and a water molecule.
In the Fe(3+) form of the Ec DOS heme PAS domain, the heme iron is ligated by His-77 and a water molecule.
In the Fe(3+) form, the heme iron is ligated to a His-77 side chain and a water molecule.
In the Fe(3+) form of the Ec DOS heme PAS domain, the heme iron is ligated by His-77 and a water molecule.
In the Fe(3+) form, the heme iron is ligated to a His-77 side chain and a water molecule.
In the Fe(3+) form of the Ec DOS heme PAS domain, the heme iron is ligated by His-77 and a water molecule.
In the Fe(3+) form, the heme iron is ligated to a His-77 side chain and a water molecule.
In the Fe(3+) form of the Ec DOS heme PAS domain, the heme iron is ligated by His-77 and a water molecule.
In the Fe(3+) form, the heme iron is ligated to a His-77 side chain and a water molecule.
In the Fe(3+) form of the Ec DOS heme PAS domain, the heme iron is ligated by His-77 and a water molecule.
In the Fe(3+) form, the heme iron is ligated to a His-77 side chain and a water molecule.
In the Fe(3+) form of the Ec DOS heme PAS domain, the heme iron is ligated by His-77 and a water molecule.
In the Fe(3+) form, the heme iron is ligated to a His-77 side chain and a water molecule.
In the Fe(3+) form of the Ec DOS heme PAS domain, the heme iron is ligated by His-77 and a water molecule.
In the Fe(3+) form, the heme iron is ligated to a His-77 side chain and a water molecule.
In the Fe(3+) form of the Ec DOS heme PAS domain, the heme iron is ligated by His-77 and a water molecule.
In the Fe(3+) form, the heme iron is ligated to a His-77 side chain and a water molecule.
In the Fe(3+) form of the Ec DOS heme PAS domain, the heme iron is ligated by His-77 and a water molecule.
In the Fe(3+) form, the heme iron is ligated to a His-77 side chain and a water molecule.
In the Fe(3+) form of the Ec DOS heme PAS domain, the heme iron is ligated by His-77 and a water molecule.
In the Fe(3+) form, the heme iron is ligated to a His-77 side chain and a water molecule.
The authors propose a redox-regulated molecular switch in which local heme-ligand switching may trigger a global scissor-type subunit movement that facilitates catalytic control.
The present data led us to propose a novel redox-regulated molecular switch in which local heme-ligand switching may trigger a global "scissor-type" subunit movement that facilitates catalytic control.
The authors propose a redox-regulated molecular switch in which local heme-ligand switching may trigger a global scissor-type subunit movement that facilitates catalytic control.
The present data led us to propose a novel redox-regulated molecular switch in which local heme-ligand switching may trigger a global "scissor-type" subunit movement that facilitates catalytic control.
The authors propose a redox-regulated molecular switch in which local heme-ligand switching may trigger a global scissor-type subunit movement that facilitates catalytic control.
The present data led us to propose a novel redox-regulated molecular switch in which local heme-ligand switching may trigger a global "scissor-type" subunit movement that facilitates catalytic control.
The authors propose a redox-regulated molecular switch in which local heme-ligand switching may trigger a global scissor-type subunit movement that facilitates catalytic control.
The present data led us to propose a novel redox-regulated molecular switch in which local heme-ligand switching may trigger a global "scissor-type" subunit movement that facilitates catalytic control.
The authors propose a redox-regulated molecular switch in which local heme-ligand switching may trigger a global scissor-type subunit movement that facilitates catalytic control.
The present data led us to propose a novel redox-regulated molecular switch in which local heme-ligand switching may trigger a global "scissor-type" subunit movement that facilitates catalytic control.
The authors propose a redox-regulated molecular switch in which local heme-ligand switching may trigger a global scissor-type subunit movement that facilitates catalytic control.
The present data led us to propose a novel redox-regulated molecular switch in which local heme-ligand switching may trigger a global "scissor-type" subunit movement that facilitates catalytic control.
The authors propose a redox-regulated molecular switch in which local heme-ligand switching may trigger a global scissor-type subunit movement that facilitates catalytic control.
The present data led us to propose a novel redox-regulated molecular switch in which local heme-ligand switching may trigger a global "scissor-type" subunit movement that facilitates catalytic control.
The authors propose a redox-regulated molecular switch in which local heme-ligand switching may trigger a global scissor-type subunit movement that facilitates catalytic control.
The present data led us to propose a novel redox-regulated molecular switch in which local heme-ligand switching may trigger a global "scissor-type" subunit movement that facilitates catalytic control.
The authors propose a redox-regulated molecular switch in which local heme-ligand switching may trigger a global scissor-type subunit movement that facilitates catalytic control.
The present data led us to propose a novel redox-regulated molecular switch in which local heme-ligand switching may trigger a global "scissor-type" subunit movement that facilitates catalytic control.
The authors propose a redox-regulated molecular switch in which local heme-ligand switching may trigger a global scissor-type subunit movement that facilitates catalytic control.
The present data led us to propose a novel redox-regulated molecular switch in which local heme-ligand switching may trigger a global "scissor-type" subunit movement that facilitates catalytic control.
The authors propose a redox-regulated molecular switch in which local heme-ligand switching may trigger a global scissor-type subunit movement that facilitates catalytic control.
The present data led us to propose a novel redox-regulated molecular switch in which local heme-ligand switching may trigger a global "scissor-type" subunit movement that facilitates catalytic control.
The authors propose a redox-regulated molecular switch in which local heme-ligand switching may trigger a global scissor-type subunit movement that facilitates catalytic control.
The present data led us to propose a novel redox-regulated molecular switch in which local heme-ligand switching may trigger a global "scissor-type" subunit movement that facilitates catalytic control.
The authors propose a redox-regulated molecular switch in which local heme-ligand switching may trigger a global scissor-type subunit movement that facilitates catalytic control.
The present data led us to propose a novel redox-regulated molecular switch in which local heme-ligand switching may trigger a global "scissor-type" subunit movement that facilitates catalytic control.
The authors propose a redox-regulated molecular switch in which local heme-ligand switching may trigger a global scissor-type subunit movement that facilitates catalytic control.
The present data led us to propose a novel redox-regulated molecular switch in which local heme-ligand switching may trigger a global "scissor-type" subunit movement that facilitates catalytic control.
The authors propose a redox-regulated molecular switch in which local heme-ligand switching may trigger a global scissor-type subunit movement that facilitates catalytic control.
The present data led us to propose a novel redox-regulated molecular switch in which local heme-ligand switching may trigger a global "scissor-type" subunit movement that facilitates catalytic control.
The authors propose a redox-regulated molecular switch in which local heme-ligand switching may trigger a global scissor-type subunit movement that facilitates catalytic control.
The present data led us to propose a novel redox-regulated molecular switch in which local heme-ligand switching may trigger a global "scissor-type" subunit movement that facilitates catalytic control.
The authors propose a redox-regulated molecular switch in which local heme-ligand switching may trigger a global scissor-type subunit movement that facilitates catalytic control.
The present data led us to propose a novel redox-regulated molecular switch in which local heme-ligand switching may trigger a global "scissor-type" subunit movement that facilitates catalytic control.
The heme PAS domain of Ec DOS forms a homodimer.
The protein folds into a characteristic PAS domain structure and forms a homodimer.
The heme PAS domain of Ec DOS forms a homodimer.
The protein folds into a characteristic PAS domain structure and forms a homodimer.
The heme PAS domain of Ec DOS forms a homodimer.
The protein folds into a characteristic PAS domain structure and forms a homodimer.
The heme PAS domain of Ec DOS forms a homodimer.
The protein folds into a characteristic PAS domain structure and forms a homodimer.
The heme PAS domain of Ec DOS forms a homodimer.
The protein folds into a characteristic PAS domain structure and forms a homodimer.
The heme PAS domain of Ec DOS forms a homodimer.
The protein folds into a characteristic PAS domain structure and forms a homodimer.
The heme PAS domain of Ec DOS forms a homodimer.
The protein folds into a characteristic PAS domain structure and forms a homodimer.
The heme PAS domain of Ec DOS forms a homodimer.
The protein folds into a characteristic PAS domain structure and forms a homodimer.
The heme PAS domain of Ec DOS forms a homodimer.
The protein folds into a characteristic PAS domain structure and forms a homodimer.
The heme PAS domain of Ec DOS forms a homodimer.
The protein folds into a characteristic PAS domain structure and forms a homodimer.
The heme PAS domain of Ec DOS forms a homodimer.
The protein folds into a characteristic PAS domain structure and forms a homodimer.
The heme PAS domain of Ec DOS forms a homodimer.
The protein folds into a characteristic PAS domain structure and forms a homodimer.
The heme PAS domain of Ec DOS forms a homodimer.
The protein folds into a characteristic PAS domain structure and forms a homodimer.
The heme PAS domain of Ec DOS forms a homodimer.
The protein folds into a characteristic PAS domain structure and forms a homodimer.
The heme PAS domain of Ec DOS forms a homodimer.
The protein folds into a characteristic PAS domain structure and forms a homodimer.
The heme PAS domain of Ec DOS forms a homodimer.
The protein folds into a characteristic PAS domain structure and forms a homodimer.
The heme PAS domain of Ec DOS forms a homodimer.
The protein folds into a characteristic PAS domain structure and forms a homodimer.
Approval Evidence
1 source5 linked approval claimsfirst-pass slug heme-pas-domain-of-ec-dos
Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms
Source:
activity state associationsupports
The heme PAS domain of Ec DOS was structurally characterized in inactive Fe(3+) and active Fe(2+) forms.
Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms at 1.32 and 1.9 A resolution, respectively.
Source:
conformational mechanismsupports
Reduction of heme iron in the Ec DOS heme PAS domain is accompanied by ligand switching from water to Met-95, FG loop rigidification, altered hydrogen bonding, and subunit rotation.
Heme iron reduction is accompanied by heme-ligand switching from the water molecule to a side chain of Met-95 from the FG loop. Concomitantly, the flexible FG loop is significantly rigidified, along with a change in the hydrogen bonding pattern and rotation of subunits relative to each other.
Source:
ligand coordinationsupports
In the Fe(3+) form of the Ec DOS heme PAS domain, the heme iron is ligated by His-77 and a water molecule.
In the Fe(3+) form, the heme iron is ligated to a His-77 side chain and a water molecule.
Source:
mechanistic modelsupports
The authors propose a redox-regulated molecular switch in which local heme-ligand switching may trigger a global scissor-type subunit movement that facilitates catalytic control.
The present data led us to propose a novel redox-regulated molecular switch in which local heme-ligand switching may trigger a global "scissor-type" subunit movement that facilitates catalytic control.
Source:
structural statesupports
The heme PAS domain of Ec DOS forms a homodimer.
The protein folds into a characteristic PAS domain structure and forms a homodimer.
Source:
Comparisons
Source-backed strengths
A key strength is direct structural characterization of both inactive Fe(3+) and active Fe(2+) forms in the same sensor domain. The evidence specifies the Fe(3+) coordination state as His-77 plus water and reports reduction-associated switching to Met-95, together with FG loop rigidification, altered hydrogen bonding, and subunit rotation.
Compared with basic helix-loop-helix (bHLH) domain
heme PAS domain of Ec DOS and basic helix-loop-helix (bHLH) domain address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: heterodimerization; same primary input modality: chemical
Compared with CIB1
heme PAS domain of Ec DOS and CIB1 address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: heterodimerization; same primary input modality: chemical
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
Compared with SMN tudor domain
heme PAS domain of Ec DOS and SMN tudor domain address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: heterodimerization; same primary input modality: chemical
Ranked Citations
- 1.