PDBsum entry 2hwv

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Transcription PDB id
Protein chain
101 a.a. *
SO4 ×3
Waters ×52
* Residue conservation analysis
PDB id:
Name: Transcription
Title: Crystal structure of an essential response regulator DNA bin domain, vicrc in enterococcus faecalis, a member of the yyc subfamily.
Structure: DNA-binding response regulator vicr. Chain: a. Fragment: c-terminal domain. Engineered: yes
Source: Enterococcus faecalis. Organism_taxid: 226185. Strain: v583. Gene: vicr. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
1.90Å     R-factor:   0.181     R-free:   0.236
Authors: C.H.Trinh,Y.Liu,S.E.V.Phillips,M.K.Phillips-Jones
Key ref:
C.H.Trinh et al. (2007). Structure of the response regulator VicR DNA-binding domain. Acta Crystallogr D Biol Crystallogr, 63, 266-269. PubMed id: 17242520 DOI: 10.1107/S0907444906043435
02-Aug-06     Release date:   23-Jan-07    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q836C2  (Q836C2_ENTFA) -  DNA-binding response regulator VicR
234 a.a.
101 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     two-component signal transduction system (phosphorelay)   2 terms 
  Biochemical function     DNA binding     1 term  


DOI no: 10.1107/S0907444906043435 Acta Crystallogr D Biol Crystallogr 63:266-269 (2007)
PubMed id: 17242520  
Structure of the response regulator VicR DNA-binding domain.
C.H.Trinh, Y.Liu, S.E.Phillips, M.K.Phillips-Jones.
The response regulator VicR from the Gram-positive bacterium Enterococcus faecalis forms part of the two-component signal transduction system of the YycFG subfamily. The structure of the DNA-binding domain of VicR, VicR(c), has been solved and belongs to the winged helix-turn-helix family. It is very similar to the DNA-binding domains of Escherichia coli PhoB and OmpR, despite low sequence similarity, but differs in two important loops. The alpha-loop, which links the two helices of the helix-turn-helix motif, is similar to that of PhoB, where it has been implicated in contacting the sigma subunit of RNA polymerase, but differs from that of OmpR. Conversely, the loop following the helix-turn-helix motif is similar to that of OmpR and differs from that of PhoB. YycF/VicR, PhoB and Bacillus subtilis PhoP regulators all recognize almost identical DNA sequences and although there is currently no experimental evidence linking this loop with the DNA, the structure is consistent with possible involvement in selective DNA recognition or binding.
  Selected figure(s)  
Figure 3.
Figure 3 Ribbon representation showing two molecules of PhoB (green) in complex with DNA shown in space-filling representation (Blanco et al., 2002[Blanco, A. G., Sola, M., Gomis-Ruth, F. X. & Coll, M. (2002). Structure, 10, 701-713.]; PDB code 1gxp ). VicR[c] is shown in red, superimposed onto one PhoB monomer. The consensus sequences for YycF/VicR homologues and PhoB targets are also shown, with the C to A/T substitution mentioned in the text indicated by red arrows in each repeat. The filled red arrow indicates the corresponding base pair in the model, which has been coloured magenta and lies close to the recognition helix. The loop region of PhoB does not reach the DNA, while the VicR[c] loop could make contact with it.
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2007, 63, 266-269) copyright 2007.  
  Figure was selected by the author.