spacer
spacer

PDBsum entry 5ieb

Go to PDB code: 
protein links
Protein PDB id
5ieb

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chain
118 a.a.
PDB id:
5ieb
Name: Protein
Title: Solution structure of sdrg from sphingomonas melonis fr1
Structure: Sensory transduction regulatory protein. Chain: a. Engineered: yes
Source: Sphingomonas melonis fr1. Organism_taxid: 1090317. Gene: sr41_04275. Expressed in: escherichia coli. Expression_system_taxid: 562
NMR struc: 20 models
Authors: S.Campagne,J.A.Vorholt,F.H.-T.Allain
Key ref: S.Campagne et al. (2016). Role of the PFXFATG[G/Y] Motif in the Activation of SdrG, a Response Regulator Involved in the Alphaproteobacterial General Stress Response. Structure, 24, 1237-1247. PubMed id: 27396826 DOI: 10.1016/j.str.2016.05.015
Date:
25-Feb-16     Release date:   20-Jul-16    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
A0A0D1MA58  (A0A0D1MA58_9SPHN) -  Sensory transduction regulatory protein from Sphingomonas melonis
Seq:
Struc:
116 a.a.
118 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1016/j.str.2016.05.015 Structure 24:1237-1247 (2016)
PubMed id: 27396826  
 
 
Role of the PFXFATG[G/Y] Motif in the Activation of SdrG, a Response Regulator Involved in the Alphaproteobacterial General Stress Response.
S.Campagne, S.Dintner, L.Gottschlich, M.Thibault, M.Bortfeld-Miller, A.Kaczmarczyk, A.Francez-Charlot, F.H.Allain, J.A.Vorholt.
 
  ABSTRACT  
 
Two-component systems are major signal transduction pathways, which consist of histidine kinases and response regulators that communicate through phosphorylation. Here, we highlight a distinct class of single-domain response regulators containing the PFXFATG[G/Y] motif that are activated by a mechanism distinct from the Y-T coupling described for prototypical receiver domains. We first solved the structures of inactive and active SdrG, a representative of the FAT GUY family, and then biochemically and genetically characterized variants in which residues in this motif were mutated. Our results support a model of activation mainly driven by a conserved lysine and reveal that the rotation of the threonine induces the reorganization of several aromatic residues in and around the PFXFATG[G/Y] motif to generate intermediates resembling those occurring during classical Y-T coupling. Overall, this helps define a new subfamily of response regulators that emerge as important players in physiological adaptation.
 

 

spacer

spacer