PDBsum entry 2pl1

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Transcriptional regulator PDB id
Protein chain
121 a.a. *
_PT ×3
Waters ×109
* Residue conservation analysis
PDB id:
Name: Transcriptional regulator
Title: Berrylium fluoride activated receiver domain of e.Coli phop
Structure: Transcriptional regulatory protein phop. Chain: a. Fragment: n-terminal regulatory domain (residues 1-121). Engineered: yes. Mutation: yes
Source: Escherichia coli. Organism_taxid: 562. Gene: phop. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
1.90Å     R-factor:   0.192     R-free:   0.226
Authors: P.Bachhawat
Key ref: P.Bachhawat and A.M.Stock (2007). Crystal structures of the receiver domain of the response regulator PhoP from Escherichia coli in the absence and presence of the phosphoryl analog beryllofluoride. J Bacteriol, 189, 5987-5995. PubMed id: 17545283
18-Apr-07     Release date:   22-May-07    
Supersedes: 2eub
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Protein chain
Pfam   ArchSchema ?
P23836  (PHOP_ECOLI) -  Transcriptional regulatory protein PhoP
223 a.a.
121 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!
  Biological process     two-component signal transduction system (phosphorelay)   1 term 
  Biochemical function     two-component response regulator activity     1 term  


J Bacteriol 189:5987-5995 (2007)
PubMed id: 17545283  
Crystal structures of the receiver domain of the response regulator PhoP from Escherichia coli in the absence and presence of the phosphoryl analog beryllofluoride.
P.Bachhawat, A.M.Stock.
The response regulator PhoP is part of the PhoQ/PhoP two-component system involved in responses to depletion of extracellular Mg(2+). Here, we report the crystal structures of the receiver domain of Escherichia coli PhoP determined in the absence and presence of the phosphoryl analog beryllofluoride. In the presence of beryllofluoride, the active receiver domain forms a twofold symmetric dimer similar to that seen in structures of other regulatory domains from the OmpR/PhoB family, providing further evidence that members of this family utilize a common mode of dimerization in the active state. In the absence of activating agents, the PhoP receiver domain crystallizes with a similar structure, consistent with the previous observation that high concentrations can promote an active state of PhoP independent of 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
20080056 R.Gao, and A.M.Stock (2010).
Molecular strategies for phosphorylation-mediated regulation of response regulator activity.
  Curr Opin Microbiol, 13, 160-167.  
19251636 J.C.Perez, and E.A.Groisman (2009).
Transcription factor function and promoter architecture govern the evolution of bacterial regulons.
  Proc Natl Acad Sci U S A, 106, 4319-4324.  
19116270 M.Weigt, R.A.White, H.Szurmant, J.A.Hoch, and T.Hwa (2009).
Identification of direct residue contacts in protein-protein interaction by message passing.
  Proc Natl Acad Sci U S A, 106, 67-72.  
19371748 T.R.Mack, R.Gao, and A.M.Stock (2009).
Probing the roles of the two different dimers mediated by the receiver domain of the response regulator PhoB.
  J Mol Biol, 389, 349-364.  
19756011 T.Schirmer, and U.Jenal (2009).
Structural and mechanistic determinants of c-di-GMP signalling.
  Nat Rev Microbiol, 7, 724-735.  
19246239 U.Jenal, and M.Y.Galperin (2009).
Single domain response regulators: molecular switches with emerging roles in cell organization and dynamics.
  Curr Opin Microbiol, 12, 152-160.  
18631241 R.Gao, Y.Tao, and A.M.Stock (2008).
System-level mapping of Escherichia coli response regulator dimerization with FRET hybrids.
  Mol Microbiol, 69, 1358-1372.  
18076904 X.Zhao, D.M.Copeland, A.S.Soares, and A.H.West (2008).
Crystal structure of a complex between the phosphorelay protein YPD1 and the response regulator domain of SLN1 bound to a phosphoryl analog.
  J Mol Biol, 375, 1141-1151.
PDB code: 2r25
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