The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis

The structure of the MarR-family transcription factor NMB1585 from Neisseria meningitidis has been solved using data extending to a resolution of 2.1 Å. Overall, the dimeric structure resembles those of other MarR proteins, with each subunit comprising a winged helix–turn–helix (wHtH) domain connect...

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Autores principales: Nichols, Charles E., Sainsbury, Sarah, Ren, Jingshan, Walter, Thomas S., Verma, Anil, Stammers, David K., Saunders, Nigel J., Owens, Raymond J.
Formato: Texto
Lenguaje:English
Publicado: International Union of Crystallography 2009
Materias:
Structural Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2650471/
https://www.ncbi.nlm.nih.gov/pubmed/19255465
http://dx.doi.org/10.1107/S174430910900414X
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author Nichols, Charles E.
Sainsbury, Sarah
Ren, Jingshan
Walter, Thomas S.
Verma, Anil
Stammers, David K.
Saunders, Nigel J.
Owens, Raymond J.
author_facet Nichols, Charles E.
Sainsbury, Sarah
Ren, Jingshan
Walter, Thomas S.
Verma, Anil
Stammers, David K.
Saunders, Nigel J.
Owens, Raymond J.
author_sort Nichols, Charles E.
collection PubMed
description The structure of the MarR-family transcription factor NMB1585 from Neisseria meningitidis has been solved using data extending to a resolution of 2.1 Å. Overall, the dimeric structure resembles those of other MarR proteins, with each subunit comprising a winged helix–turn–helix (wHtH) domain connected to an α-helical dimerization domain. The spacing of the recognition helices of the wHtH domain indicates that NMB1585 is pre-configured for DNA binding, with a putative inducer pocket that is largely occluded by the side chains of two aromatic residues (Tyr29 and Trp53). NMB1585 was shown to bind to its own promoter region in a gel-shift assay, indicating that the protein acts as an auto-repressor.
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spelling pubmed-26504712009-03-09 The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis Nichols, Charles E. Sainsbury, Sarah Ren, Jingshan Walter, Thomas S. Verma, Anil Stammers, David K. Saunders, Nigel J. Owens, Raymond J. Acta Crystallogr Sect F Struct Biol Cryst Commun Structural Communications The structure of the MarR-family transcription factor NMB1585 from Neisseria meningitidis has been solved using data extending to a resolution of 2.1 Å. Overall, the dimeric structure resembles those of other MarR proteins, with each subunit comprising a winged helix–turn–helix (wHtH) domain connected to an α-helical dimerization domain. The spacing of the recognition helices of the wHtH domain indicates that NMB1585 is pre-configured for DNA binding, with a putative inducer pocket that is largely occluded by the side chains of two aromatic residues (Tyr29 and Trp53). NMB1585 was shown to bind to its own promoter region in a gel-shift assay, indicating that the protein acts as an auto-repressor. International Union of Crystallography 2009-02-26 /pmc/articles/PMC2650471/ /pubmed/19255465 http://dx.doi.org/10.1107/S174430910900414X Text en © Nichols et al. 2009 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Structural Communications
Nichols, Charles E.
Sainsbury, Sarah
Ren, Jingshan
Walter, Thomas S.
Verma, Anil
Stammers, David K.
Saunders, Nigel J.
Owens, Raymond J.
The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis
title The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis
title_full The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis
title_fullStr The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis
title_full_unstemmed The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis
title_short The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis
title_sort structure of nmb1585, a marr-family regulator from neisseria meningitidis
topic Structural Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2650471/
https://www.ncbi.nlm.nih.gov/pubmed/19255465
http://dx.doi.org/10.1107/S174430910900414X
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