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PDBsum entry 1mb3
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protein metals links
Signaling protein, cell cycle PDB id
1mb3

 

 

 

 

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Contents
Protein chain
117 a.a. *
Metals
_MG
Waters ×63
* Residue conservation analysis
PDB id:
1mb3
Name: Signaling protein, cell cycle
Title: Crystal structure of the response regulator divk at ph 8.5 in complex with mg2+
Structure: Cell division response regulator divk. Chain: a. Synonym: polar differentiation response regulator, divk response regulator. Engineered: yes
Source: Caulobacter vibrioides. Organism_taxid: 155892. Gene: divk. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.41Å     R-factor:   0.207     R-free:   0.215
Authors: V.Guillet,N.Ohta,S.Cabantous,A.Newton,J.-P.Samama,Structural Proteomics In Europe (Spine)
Key ref:
V.Guillet et al. (2002). Crystallographic and biochemical studies of DivK reveal novel features of an essential response regulator in Caulobacter crescentus. J Biol Chem, 277, 42003-42010. PubMed id: 12176983 DOI: 10.1074/jbc.M204789200
Date:
02-Aug-02     Release date:   04-Dec-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Q9A5I4  (Q9A5I4_CAUVC) -  Polar differentiation response regulator from Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15)
Seq:
Struc: 		130 a.a.
117 a.a.
Key:    Secondary structure  CATH domain

 

 
DOI no: 10.1074/jbc.M204789200 J Biol Chem 277:42003-42010 (2002)
PubMed id: 12176983  
 
 
Crystallographic and biochemical studies of DivK reveal novel features of an essential response regulator in Caulobacter crescentus.
V.Guillet, N.Ohta, S.Cabantous, A.Newton, J.P.Samama.
 
  ABSTRACT  
 
DivK is an essential response regulator in the Gram-negative bacterium Caulobacter crescentus and functions in a complex phosphorelay system that precisely controls the sequence of developmental events during the cell division cycle. Structure determinations of this single domain response regulator at different pH values demonstrated that the five-stranded alpha/beta fold of the DivK protein is fully defined only at acidic pH. The crystal structures of the apoprotein and of metal-bound DivK complexes at higher pH values revealed a synergistic pH- and cation binding-induced flexibility of the beta4-alpha4 loop and of the alpha4 helix. This motion increases the solvent accessibility of the single cysteine residue in the protein. Solution state studies demonstrated a 200-fold pH-dependent increase in the affinity of manganese for the protein between pH 6.0 and 8.5 that seems to involve deprotonation of an acido-basic couple. Taken together, these results suggest that flexibility of critical regions of the protein, ionization of the cysteine 99 residue and improved K(D) values for the catalytic metal ion are coupled events. We propose that the molecular events observed in the isolated protein may be required for DivK activation and that they may be achieved in vivo through the specific protein-protein interactions between the response regulator and its cognate kinases.
 
  Selected figure(s)  
 
Figure 4.
Fig. 4. Stereoview of the 2F[o] F[c] electron density map in the active site region for the Mn2+-DivK complex at pH 8.0. 		Figure 6.
Fig. 6. CA representation of the DivK structure illustrating by dotted line the non visible region (residues 84-97) when the metal binds with high affinity.
 
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2002, 277, 42003-42010) copyright 2002.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20361049 J.O.Wrabl, and V.J.Hilser (2010).
Investigating homology between proteins using energetic profiles.
  PLoS Comput Biol, 6, e1000722.  
20197497 P.D.Curtis, and Y.V.Brun (2010).
Getting in the loop: regulation of development in Caulobacter crescentus.
  Microbiol Mol Biol Rev, 74, 13-41.  
20211578 R.B.Bourret (2010).
Receiver domain structure and function in response regulator proteins.
  Curr Opin Microbiol, 13, 142-149.  
16929106 M.Solà, D.L.Drew, A.G.Blanco, F.X.Gomis-Rüth, and M.Coll (2006).
The cofactor-induced pre-active conformation in PhoB.
  Acta Crystallogr D Biol Crystallogr, 62, 1046-1057.
PDB code: 2iyn
15039551 D.Mukhopadhyay, U.Sen, J.Zapf, and K.I.Varughese (2004).
Metals in the sporulation phosphorelay: manganese binding by the response regulator Spo0F.
  Acta Crystallogr D Biol Crystallogr, 60, 638-645.
PDB code: 1pey
14662348 E.M.Quardokus, and Y.V.Brun (2003).
Cell cycle timing and developmental checkpoints in Caulobacter crescentus.
  Curr Opin Microbiol, 6, 541-549.  
12562781 L.Kroos, and J.R.Maddock (2003).
Prokaryotic development: emerging insights.
  J Bacteriol, 185, 1128-1146.  
14527278 N.Ausmees, and C.Jacobs-Wagner (2003).
Spatial and temporal control of differentiation and cell cycle progression in Caulobacter crescentus.
  Annu Rev Microbiol, 57, 225-247.  
12867451 N.Ohta, and A.Newton (2003).
The core dimerization domains of histidine kinases contain recognition specificity for the cognate response regulator.
  J Bacteriol, 185, 4424-4431.  
12457698 U.Jenal, and C.Stephens (2002).
The Caulobacter cell cycle: timing, spatial organization and checkpoints.
  Curr Opin Microbiol, 5, 558-563.  
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 code is shown on the right.

 

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