Source 1primary paper2006Biochemistry
Toolkit/EAL domain of YcgF
EAL domain of YcgF
Also known as: C-terminal EAL domain
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The Escherichia coli YcgF protein contains a C-terminal EAL domain linked to an N-terminal FAD-binding BLUF photosensory domain. In this full-length blue-light-responsive protein context, the EAL domain is predicted to have cyclic-di-GMP phosphodiesterase activity.
Usefulness & Problems
Why this is useful
This domain is useful as part of a naturally occurring light-responsive signaling protein architecture that couples a BLUF photosensory module to a putative EAL output module. The available evidence supports relevance to blue-light-regulated signaling, but does not directly establish standalone tool performance for engineering applications.
Problem solved
It addresses the biological problem of linking blue-light sensing to a predicted cyclic-di-GMP signaling output within a single Escherichia coli protein. The evidence does not show direct experimental demonstration that the isolated EAL domain alone solves a specific engineering control problem.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
blue-light sensing via a bluf-associated fad chromophorelight-induced conformational changepredicted cyclic-di-gmp phosphodiesterase activityTechniques
Structural CharacterizationTarget processes
signalingInput: Light
Implementation Constraints
The full-length YcgF protein is from Escherichia coli and contains an N-terminal FAD-binding BLUF domain fused to the C-terminal EAL domain. FAD is therefore an associated chromophore in the native photosensory context, but the supplied evidence does not specify construct design, expression conditions, or whether the EAL domain is functional when isolated.
The cyclic-di-GMP phosphodiesterase function of the EAL domain is described as predicted rather than directly demonstrated in the supplied evidence. The evidence also does not provide direct validation of light-regulated catalytic activity, isolated EAL-domain behavior, kinetic parameters, or use in heterologous systems.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
The C4=O stretching bands of the FAD isoalloxazine ring were induced at the same frequency and with the same band intensity in YcgF-Full and YcgF-BLUF spectra.
the bands for the C4=O stretching of a FAD isoalloxazine ring were induced at the same frequency with the same band intensity in the spectra for YcgF-Full and YcgF-BLUF
The C4=O stretching bands of the FAD isoalloxazine ring were induced at the same frequency and with the same band intensity in YcgF-Full and YcgF-BLUF spectra.
the bands for the C4=O stretching of a FAD isoalloxazine ring were induced at the same frequency with the same band intensity in the spectra for YcgF-Full and YcgF-BLUF
The C4=O stretching bands of the FAD isoalloxazine ring were induced at the same frequency and with the same band intensity in YcgF-Full and YcgF-BLUF spectra.
the bands for the C4=O stretching of a FAD isoalloxazine ring were induced at the same frequency with the same band intensity in the spectra for YcgF-Full and YcgF-BLUF
The C4=O stretching bands of the FAD isoalloxazine ring were induced at the same frequency and with the same band intensity in YcgF-Full and YcgF-BLUF spectra.
the bands for the C4=O stretching of a FAD isoalloxazine ring were induced at the same frequency with the same band intensity in the spectra for YcgF-Full and YcgF-BLUF
The C4=O stretching bands of the FAD isoalloxazine ring were induced at the same frequency and with the same band intensity in YcgF-Full and YcgF-BLUF spectra.
the bands for the C4=O stretching of a FAD isoalloxazine ring were induced at the same frequency with the same band intensity in the spectra for YcgF-Full and YcgF-BLUF
The C4=O stretching bands of the FAD isoalloxazine ring were induced at the same frequency and with the same band intensity in YcgF-Full and YcgF-BLUF spectra.
the bands for the C4=O stretching of a FAD isoalloxazine ring were induced at the same frequency with the same band intensity in the spectra for YcgF-Full and YcgF-BLUF
The C4=O stretching bands of the FAD isoalloxazine ring were induced at the same frequency and with the same band intensity in YcgF-Full and YcgF-BLUF spectra.
the bands for the C4=O stretching of a FAD isoalloxazine ring were induced at the same frequency with the same band intensity in the spectra for YcgF-Full and YcgF-BLUF
Escherichia coli YcgF is a BLUF protein composed of an N-terminal BLUF domain and a C-terminal EAL domain.
The Escherichia coli YcgF protein is a BLUF protein consisting of the N-terminal FAD-binding hold (BLUF domain) and the C-terminal EAL domain.
Escherichia coli YcgF is a BLUF protein composed of an N-terminal BLUF domain and a C-terminal EAL domain.
The Escherichia coli YcgF protein is a BLUF protein consisting of the N-terminal FAD-binding hold (BLUF domain) and the C-terminal EAL domain.
Escherichia coli YcgF is a BLUF protein composed of an N-terminal BLUF domain and a C-terminal EAL domain.
The Escherichia coli YcgF protein is a BLUF protein consisting of the N-terminal FAD-binding hold (BLUF domain) and the C-terminal EAL domain.
Escherichia coli YcgF is a BLUF protein composed of an N-terminal BLUF domain and a C-terminal EAL domain.
The Escherichia coli YcgF protein is a BLUF protein consisting of the N-terminal FAD-binding hold (BLUF domain) and the C-terminal EAL domain.
Escherichia coli YcgF is a BLUF protein composed of an N-terminal BLUF domain and a C-terminal EAL domain.
The Escherichia coli YcgF protein is a BLUF protein consisting of the N-terminal FAD-binding hold (BLUF domain) and the C-terminal EAL domain.
Escherichia coli YcgF is a BLUF protein composed of an N-terminal BLUF domain and a C-terminal EAL domain.
The Escherichia coli YcgF protein is a BLUF protein consisting of the N-terminal FAD-binding hold (BLUF domain) and the C-terminal EAL domain.
Escherichia coli YcgF is a BLUF protein composed of an N-terminal BLUF domain and a C-terminal EAL domain.
The Escherichia coli YcgF protein is a BLUF protein consisting of the N-terminal FAD-binding hold (BLUF domain) and the C-terminal EAL domain.
The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.
The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.
The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.
The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.
The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.
The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.
The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.
The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.
The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.
The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.
The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.
The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.
The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.
The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.
The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.
The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.
The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.
The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.
The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.
The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.
The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.
The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.
The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.
The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.
The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.
The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.
The light-induced FTIR difference spectrum of full-length YcgF was markedly different from that of the isolated YcgF BLUF domain, and the BLUF-domain spectrum lacked most IR bands induced in the full-length protein.
The light-induced FTIR difference spectrum of YcgF-Full, however, was markedly different from that of YcgF-BLUF. The spectrum of YcgF-BLUF lacked most of the IR bands that were induced in the YcgF-Full spectrum.
YcgF-Full and YcgF-BLUF showed identical dark-state flavin UV-visible absorption spectra and identical kinetics of relaxation from the light-induced signaling state to the dark state.
YcgF-Full and YcgF-BLUF showed identical UV-visible absorption spectra of flavin in the dark state and a light-induced absorption red shift for the signaling state, which relaxed to the dark state showing identical kinetics.
YcgF-Full and YcgF-BLUF showed identical dark-state flavin UV-visible absorption spectra and identical kinetics of relaxation from the light-induced signaling state to the dark state.
YcgF-Full and YcgF-BLUF showed identical UV-visible absorption spectra of flavin in the dark state and a light-induced absorption red shift for the signaling state, which relaxed to the dark state showing identical kinetics.
YcgF-Full and YcgF-BLUF showed identical dark-state flavin UV-visible absorption spectra and identical kinetics of relaxation from the light-induced signaling state to the dark state.
YcgF-Full and YcgF-BLUF showed identical UV-visible absorption spectra of flavin in the dark state and a light-induced absorption red shift for the signaling state, which relaxed to the dark state showing identical kinetics.
YcgF-Full and YcgF-BLUF showed identical dark-state flavin UV-visible absorption spectra and identical kinetics of relaxation from the light-induced signaling state to the dark state.
YcgF-Full and YcgF-BLUF showed identical UV-visible absorption spectra of flavin in the dark state and a light-induced absorption red shift for the signaling state, which relaxed to the dark state showing identical kinetics.
YcgF-Full and YcgF-BLUF showed identical dark-state flavin UV-visible absorption spectra and identical kinetics of relaxation from the light-induced signaling state to the dark state.
YcgF-Full and YcgF-BLUF showed identical UV-visible absorption spectra of flavin in the dark state and a light-induced absorption red shift for the signaling state, which relaxed to the dark state showing identical kinetics.
YcgF-Full and YcgF-BLUF showed identical dark-state flavin UV-visible absorption spectra and identical kinetics of relaxation from the light-induced signaling state to the dark state.
YcgF-Full and YcgF-BLUF showed identical UV-visible absorption spectra of flavin in the dark state and a light-induced absorption red shift for the signaling state, which relaxed to the dark state showing identical kinetics.
YcgF-Full and YcgF-BLUF showed identical dark-state flavin UV-visible absorption spectra and identical kinetics of relaxation from the light-induced signaling state to the dark state.
YcgF-Full and YcgF-BLUF showed identical UV-visible absorption spectra of flavin in the dark state and a light-induced absorption red shift for the signaling state, which relaxed to the dark state showing identical kinetics.
The full-length-specific protein bands are discussed as being predominantly attributable to structural changes in the C-terminal EAL domain triggered by light excitation of the N-terminal BLUF domain.
The possibility that full-length-specific protein bands are predominantly ascribed to structural changes of the C-terminal EAL domain in the signaling state as a consequence of light excitation of the N-terminal BLUF domain is discussed.
The full-length-specific protein bands are discussed as being predominantly attributable to structural changes in the C-terminal EAL domain triggered by light excitation of the N-terminal BLUF domain.
The possibility that full-length-specific protein bands are predominantly ascribed to structural changes of the C-terminal EAL domain in the signaling state as a consequence of light excitation of the N-terminal BLUF domain is discussed.
The full-length-specific protein bands are discussed as being predominantly attributable to structural changes in the C-terminal EAL domain triggered by light excitation of the N-terminal BLUF domain.
The possibility that full-length-specific protein bands are predominantly ascribed to structural changes of the C-terminal EAL domain in the signaling state as a consequence of light excitation of the N-terminal BLUF domain is discussed.
The full-length-specific protein bands are discussed as being predominantly attributable to structural changes in the C-terminal EAL domain triggered by light excitation of the N-terminal BLUF domain.
The possibility that full-length-specific protein bands are predominantly ascribed to structural changes of the C-terminal EAL domain in the signaling state as a consequence of light excitation of the N-terminal BLUF domain is discussed.
The full-length-specific protein bands are discussed as being predominantly attributable to structural changes in the C-terminal EAL domain triggered by light excitation of the N-terminal BLUF domain.
The possibility that full-length-specific protein bands are predominantly ascribed to structural changes of the C-terminal EAL domain in the signaling state as a consequence of light excitation of the N-terminal BLUF domain is discussed.
The full-length-specific protein bands are discussed as being predominantly attributable to structural changes in the C-terminal EAL domain triggered by light excitation of the N-terminal BLUF domain.
The possibility that full-length-specific protein bands are predominantly ascribed to structural changes of the C-terminal EAL domain in the signaling state as a consequence of light excitation of the N-terminal BLUF domain is discussed.
The full-length-specific protein bands are discussed as being predominantly attributable to structural changes in the C-terminal EAL domain triggered by light excitation of the N-terminal BLUF domain.
The possibility that full-length-specific protein bands are predominantly ascribed to structural changes of the C-terminal EAL domain in the signaling state as a consequence of light excitation of the N-terminal BLUF domain is discussed.
At medium-low temperatures, the YcgF-Full FTIR spectrum resembled the YcgF-BLUF spectrum because protein bands were selectively suppressed.
the YcgF-Full spectrum resembled that of the YcgF-BLUF when illuminated at medium-low temperatures because of the selective suppression of protein bands
At medium-low temperatures, the YcgF-Full FTIR spectrum resembled the YcgF-BLUF spectrum because protein bands were selectively suppressed.
the YcgF-Full spectrum resembled that of the YcgF-BLUF when illuminated at medium-low temperatures because of the selective suppression of protein bands
At medium-low temperatures, the YcgF-Full FTIR spectrum resembled the YcgF-BLUF spectrum because protein bands were selectively suppressed.
the YcgF-Full spectrum resembled that of the YcgF-BLUF when illuminated at medium-low temperatures because of the selective suppression of protein bands
At medium-low temperatures, the YcgF-Full FTIR spectrum resembled the YcgF-BLUF spectrum because protein bands were selectively suppressed.
the YcgF-Full spectrum resembled that of the YcgF-BLUF when illuminated at medium-low temperatures because of the selective suppression of protein bands
At medium-low temperatures, the YcgF-Full FTIR spectrum resembled the YcgF-BLUF spectrum because protein bands were selectively suppressed.
the YcgF-Full spectrum resembled that of the YcgF-BLUF when illuminated at medium-low temperatures because of the selective suppression of protein bands
At medium-low temperatures, the YcgF-Full FTIR spectrum resembled the YcgF-BLUF spectrum because protein bands were selectively suppressed.
the YcgF-Full spectrum resembled that of the YcgF-BLUF when illuminated at medium-low temperatures because of the selective suppression of protein bands
At medium-low temperatures, the YcgF-Full FTIR spectrum resembled the YcgF-BLUF spectrum because protein bands were selectively suppressed.
the YcgF-Full spectrum resembled that of the YcgF-BLUF when illuminated at medium-low temperatures because of the selective suppression of protein bands
Approval Evidence
1 source3 linked approval claimsfirst-pass slug eal-domain-of-ycgf
The Escherichia coli YcgF protein is a BLUF protein consisting of the N-terminal FAD-binding hold (BLUF domain) and the C-terminal EAL domain. The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.
Source:
compositionsupports
Escherichia coli YcgF is a BLUF protein composed of an N-terminal BLUF domain and a C-terminal EAL domain.
The Escherichia coli YcgF protein is a BLUF protein consisting of the N-terminal FAD-binding hold (BLUF domain) and the C-terminal EAL domain.
Source:
predicted activitysupports
The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.
The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.
Source:
structural interpretationneutral
The full-length-specific protein bands are discussed as being predominantly attributable to structural changes in the C-terminal EAL domain triggered by light excitation of the N-terminal BLUF domain.
The possibility that full-length-specific protein bands are predominantly ascribed to structural changes of the C-terminal EAL domain in the signaling state as a consequence of light excitation of the N-terminal BLUF domain is discussed.
Source:
Comparisons
Source-backed strengths
YcgF has a defined modular composition, with an N-terminal BLUF domain and a C-terminal EAL domain, which supports interpretation as a sensory-output fusion protein. FTIR difference spectroscopy showed that FAD isoalloxazine C4=O stretching bands were induced at the same frequency and intensity in full-length YcgF and the isolated BLUF region, supporting characterized light-induced changes in the photosensory portion of the protein.
Ranked Citations
- 1.