spacer
spacer
Go to PDB code: 
protein Protein-protein interface(s) links
Signaling protein PDB id
3g6b
Jmol
Contents
Protein chains
213 a.a. *
Waters ×416
* Residue conservation analysis
PDB id:
3g6b
Name: Signaling protein
Title: Crystal structure of a soluble chemoreceptor from thermotoga maritima asn217ile mutant
Structure: Methyl-accepting chemotaxis protein. Chain: a, b. Engineered: yes. Mutation: yes
Source: Thermotoga maritima. Organism_taxid: 2336. Gene: tm0014, tm_0014. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
3.00Å     R-factor:   0.259     R-free:   0.305
Authors: A.M.Pollard,A.M.Bilwes,B.R.Crane
Key ref: A.Pollard et al. (2009). Structure of a soluble chemoreceptor suggests a mechanism for propagating conformational signals. Biochemistry, 48, 1936-1944. PubMed id: 19149470 DOI: 10.1021/bi801727m
Date:
06-Feb-09     Release date:   28-Jul-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q7DFA3  (Q7DFA3_THEMA) -  Methyl-accepting chemotaxis protein, putative
Seq:
Struc: 		278 a.a.
213 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   1 term 
  Biological process     signal transduction   1 term 
  Biochemical function     signal transducer activity     1 term  

 

 
DOI no: 10.1021/bi801727m Biochemistry 48:1936-1944 (2009)
PubMed id: 19149470  
 
 
Structure of a soluble chemoreceptor suggests a mechanism for propagating conformational signals.
A.Pollard, A.Bilwes, B.Crane.
 
  ABSTRACT  
 
Transmembrane chemoreceptors, also known as methyl-accepting chemotaxis proteins (MCPs), translate extracellular signals into intracellular responses in the bacterial chemotaxis system. MCP ligand binding domains control the activity of the CheA kinase, situated ~200 ? away, across the cytoplasmic membrane. The 2.15 ? resolution crystal structure of a T. maritima soluble receptor (Tm14) reveals distortions in its dimeric four-helix bundle that provide insight into the conformational states available to MCPs for propagating signals. A bulge in one helix generates asymmetry between subunits that displaces the kinase-interacting tip, which resides over 100 ? away. The maximum bundle distortion maps to the adaptation region of transmembrane MCPs where reversible methylation of acidic residues tunes receptor activity. Minor alterations in coiled-coil packing geometry translates the bulge distortion to a >25 ? movement of the tip relative to the bundle stalks. The Tm14 structure discloses how alterations in local helical structure, which could be induced by changes in methylation state and/or by conformational signals from membrane proximal regions, can reposition a remote domain that interacts with the CheA kinase.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21087385 T.Krell, J.Lacal, F.Muñoz-Martínez, J.A.Reyes-Darias, B.H.Cadirci, C.García-Fontana, and J.L.Ramos (2011).
Diversity at its best: bacterial taxis.
  Environ Microbiol, 13, 1115-1124.  
20088541 D.J.Fowler, R.M.Weis, and L.K.Thompson (2010).
Kinase-active signaling complexes of bacterial chemoreceptors do not contain proposed receptor-receptor contacts observed in crystal structures.
  Biochemistry, 49, 1425-1434.  
21091513 D.N.Amin, and G.L.Hazelbauer (2010).
Chemoreceptors in signalling complexes: shifted conformation and asymmetric coupling.
  Mol Microbiol, 78, 1313-1323.  
20355710 J.Bhatnagar, P.P.Borbat, A.M.Pollard, A.M.Bilwes, J.H.Freed, and B.R.Crane (2010).
Structure of the ternary complex formed by a chemotaxis receptor signaling domain, the CheA histidine kinase, and the coupling protein CheW as determined by pulsed dipolar ESR spectroscopy.
  Biochemistry, 49, 3824-3841.  
20738376 J.Lacal, C.García-Fontana, F.Muñoz-Martínez, J.L.Ramos, and T.Krell (2010).
Sensing of environmental signals: classification of chemoreceptors according to the size of their ligand binding regions.
  Environ Microbiol, 12, 2873-2884.  
19496930 B.E.Scharf, P.D.Aldridge, J.R.Kirby, and B.R.Crane (2009).
Upward mobility and alternative lifestyles: a report from the 10th biennial meeting on Bacterial Locomotion and Signal Transduction.
  Mol Microbiol, 73, 5.  
19805278 D.Albanesi, M.Martín, F.Trajtenberg, M.C.Mansilla, A.Haouz, P.M.Alzari, D.de Mendoza, and A.Buschiazzo (2009).
Structural plasticity and catalysis regulation of a thermosensor histidine kinase.
  Proc Natl Acad Sci U S A, 106, 16185-16190.
PDB codes: 3ehf 3ehh 3ehj 3gie 3gif 3gig
19705835 K.E.Swain, M.A.Gonzalez, and J.J.Falke (2009).
Engineered socket study of signaling through a four-helix bundle: evidence for a yin-yang mechanism in the kinase control module of the aspartate receptor.
  Biochemistry, 48, 9266-9277.  
19656294 Q.Zhou, P.Ames, and J.S.Parkinson (2009).
Mutational analyses of HAMP helices suggest a dynamic bundle model of input-output signalling in chemoreceptors.
  Mol Microbiol, 73, 801-814.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.