Structure of the response regulator VicR DNA-binding domain

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, VicRc, has been solved and belongs to the winged helix–turn–helix family. It is very...

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Veröffentlicht in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2007-02, Vol.63 (2), p.266-269
Hauptverfasser: Trinh, Chi-Hung, Liu, Yang, Phillips, Simon E. V., Phillips-Jones, Mary K.
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Sprache:eng
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Zusammenfassung: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, VicRc, 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 α‐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 σ 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.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444906043435