2HWV

Crystal structure of an essential response regulator DNA binding domain, VicRc in Enterococcus faecalis, a member of the YycF subfamily.

Summary for 2HWV

• Entry DOI: 10.2210/pdb2hwv/pdb
• Descriptor: DNA-binding response regulator VicR, SULFATE ION (3 entities in total)
• Functional Keywords: essential response regulator, c-terminal domain, dna-binding domain, transcription
• Biological source: Enterococcus faecalis
• Total number of polymer chains: 1
• Total formula weight: 14478.23

Authors

Trinh, C.H.,Liu, Y.,Phillips, S.E.V.,Phillips-Jones, M.K. (deposition date: 2006-08-02, release date: 2007-01-23, Last modification date: 2023-09-20)

Primary citation

Trinh, C.H.,Liu, Y.,Phillips, S.E.,Phillips-Jones, M.K.
Structure of the response regulator VicR DNA-binding domain.
Acta Crystallogr.,Sect.D, 63:266-269, 2007

PubMed Abstract: 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.

PubMed: 17242520
DOI: 10.1107/S0907444906043435

Experimental method

X-RAY DIFFRACTION (1.9 Å)