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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, VicR(c), has been solved and belongs to the winged helix–turn–helix family. It is ver...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2007
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2483477/ https://www.ncbi.nlm.nih.gov/pubmed/17242520 http://dx.doi.org/10.1107/S0907444906043435 |
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author | Trinh, Chi-Hung Liu, Yang Phillips, Simon E. V. Phillips-Jones, Mary K. |
author_facet | Trinh, Chi-Hung Liu, Yang Phillips, Simon E. V. Phillips-Jones, Mary K. |
author_sort | Trinh, Chi-Hung |
collection | PubMed |
description | 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 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. |
format | Text |
id | pubmed-2483477 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-24834772009-03-05 Structure of the response regulator VicR DNA-binding domain Trinh, Chi-Hung Liu, Yang Phillips, Simon E. V. Phillips-Jones, Mary K. Acta Crystallogr D Biol Crystallogr Short Communications 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 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. International Union of Crystallography 2007-02-01 2007-01-16 /pmc/articles/PMC2483477/ /pubmed/17242520 http://dx.doi.org/10.1107/S0907444906043435 Text en © International Union of Crystallography 2007 http://journals.iucr.org/services/termsofuse.html This is an open-access article distributed under the terms described at http://journals.iucr.org/services/termsofuse.html. |
spellingShingle | Short Communications Trinh, Chi-Hung Liu, Yang Phillips, Simon E. V. Phillips-Jones, Mary K. Structure of the response regulator VicR DNA-binding domain |
title | Structure of the response regulator VicR DNA-binding domain |
title_full | Structure of the response regulator VicR DNA-binding domain |
title_fullStr | Structure of the response regulator VicR DNA-binding domain |
title_full_unstemmed | Structure of the response regulator VicR DNA-binding domain |
title_short | Structure of the response regulator VicR DNA-binding domain |
title_sort | structure of the response regulator vicr dna-binding domain |
topic | Short Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2483477/ https://www.ncbi.nlm.nih.gov/pubmed/17242520 http://dx.doi.org/10.1107/S0907444906043435 |
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