PDBsum entry 2gkg

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protein links
Signaling protein PDB id
Protein chain
122 a.a. *
Waters ×362
* Residue conservation analysis
PDB id:
Name: Signaling protein
Title: Receiver domain from myxococcus xanthus social motility prot
Structure: Response regulator homolog. Chain: a. Fragment: receiver domain (residues 1-124). Engineered: yes
Source: Myxococcus xanthus. Organism_taxid: 34. Gene: frzs. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
1.00Å     R-factor:   0.092     R-free:   0.123
Authors: N.Echols,J.Fraser,J.Merlie,D.Zusman,T.Alber
Key ref: J.S.Fraser et al. (2007). An atypical receiver domain controls the dynamic polar localization of the Myxococcus xanthus social motility protein FrzS. Mol Microbiol, 65, 319-332. PubMed id: 17573816
01-Apr-06     Release date:   13-Mar-07    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
O68522  (O68522_MYXXA) -  Response regulator homolog
562 a.a.
122 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     two-component signal transduction system (phosphorelay)   1 term 


Mol Microbiol 65:319-332 (2007)
PubMed id: 17573816  
An atypical receiver domain controls the dynamic polar localization of the Myxococcus xanthus social motility protein FrzS.
J.S.Fraser, J.P.Merlie, N.Echols, S.R.Weisfield, T.Mignot, D.E.Wemmer, D.R.Zusman, T.Alber.
The Myxococcus xanthus FrzS protein transits from pole-to-pole within the cell, accumulating at the pole that defines the direction of movement in social (S) motility. Here we show using atomic-resolution crystallography and NMR that the FrzS receiver domain (RD) displays the conserved switch Tyr102 in an unusual conformation, lacks the conserved Asp phosphorylation site, and fails to bind Mg(2+) or the phosphoryl analogue, Mg(2+) x BeF(3). Mutation of Asp55, closest to the canonical site of RD phosphorylation, showed no motility phenotype in vivo, demonstrating that phosphorylation at this site is not necessary for domain function. In contrast, the Tyr102Ala and His92Phe substitutions on the canonical output face of the FrzS RD abolished S-motility in vivo. Single-cell fluorescence microscopy measurements revealed a striking mislocalization of these mutant FrzS proteins to the trailing cell pole in vivo. The crystal structures of the mutants suggested that the observed conformation of Tyr102 in the wild-type FrzS RD is not sufficient for function. These results support the model that FrzS contains a novel 'pseudo-receiver domain' whose function requires recognition of the RD output face but not Asp phosphorylation.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20702407 C.M.Barbieri, T.R.Mack, V.L.Robinson, M.T.Miller, and A.M.Stock (2010).
Regulation of response regulator autophosphorylation through interdomain contacts.
  J Biol Chem, 285, 32325-32335.
PDB codes: 3nhz 3nnn 3nns
20862323 H.Xu, M.J.Caimano, T.Lin, M.He, J.D.Radolf, S.J.Norris, F.Gheradini, A.J.Wolfe, and X.F.Yang (2010).
Role of acetyl-phosphate in activation of the Rrp2-RpoN-RpoS pathway in Borrelia burgdorferi.
  PLoS Pathog, 6, 0.  
20211578 R.B.Bourret (2010).
Receiver domain structure and function in response regulator proteins.
  Curr Opin Microbiol, 13, 142-149.  
20063153 U.M.Hohenester, K.Ludwig, J.Krieglstein, and S.König (2010).
Stepchild phosphohistidine: acid-labile phosphorylation becomes accessible by functional proteomics.
  Anal Bioanal Chem, 397, 3209-3212.  
19124574 J.F.Mariscotti, and F.García-del Portillo (2009).
Genome expression analyses revealing the modulation of the Salmonella Rcs regulon by the attenuator IgaA.
  J Bacteriol, 191, 1855-1867.  
19423672 L.Wang, X.Tian, J.Wang, H.Yang, K.Fan, G.Xu, K.Yang, and H.Tan (2009).
Autoregulation of antibiotic biosynthesis by binding of the end product to an atypical response regulator.
  Proc Natl Acad Sci U S A, 106, 8617-8622.  
18832306 D.Ruiz, P.Salinas, M.L.Lopez-Redondo, M.L.Cayuela, A.Marina, and A.Contreras (2008).
Phosphorylation-independent activation of the atypical response regulator NblR.
  Microbiology, 154, 3002-3015.  
18623059 T.Mignot, and J.R.Kirby (2008).
Genetic circuitry controlling motility behaviors of Myxococcus xanthus.
  Bioessays, 30, 733-743.  
17922045 D.R.Zusman, A.E.Scott, Z.Yang, and J.R.Kirby (2007).
Chemosensory pathways, motility and development in Myxococcus xanthus.
  Nat Rev Microbiol, 5, 862-872.  
17981496 E.M.Mauriello, and D.R.Zusman (2007).
Polarity of motility systems in Myxococcus xanthus.
  Curr Opin Microbiol, 10, 624-629.  
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.