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DC Field | Value | Language |
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dc.contributor.author | Nichols, CE | - |
dc.contributor.author | Sainsbury, S | - |
dc.contributor.author | Ren, J | - |
dc.contributor.author | Walter, TS | - |
dc.contributor.author | Verma, A | - |
dc.contributor.author | Stammers, DK | - |
dc.contributor.author | Saunders, NJ | - |
dc.contributor.author | Owens, RJ | - |
dc.date.accessioned | 2012-09-14T12:17:15Z | - |
dc.date.available | 2012-09-14T12:17:15Z | - |
dc.date.issued | 2009 | - |
dc.identifier.citation | Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 65(Pt 3): 204 - 209, Mar 2009 | en_US |
dc.identifier.issn | 1744-3091 | - |
dc.identifier.uri | http://onlinelibrary.wiley.com/doi/10.1107/S174430910900414X/abstract | en |
dc.identifier.uri | http://bura.brunel.ac.uk/handle/2438/6645 | - |
dc.description | Copyright @ 2009 Nichols et al. | en_US |
dc.description.abstract | 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. | en_US |
dc.description.sponsorship | This work is funded by the UK Medical Research Council and The Biotechnology Biochemical Research Council | en_US |
dc.language.iso | en | en_US |
dc.publisher | International Union of Crystallography | en_US |
dc.subject | MarR | en_US |
dc.subject | Neisseria meningitidis | en_US |
dc.subject | Transcription factors | en_US |
dc.title | The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis | en_US |
dc.type | Article | en_US |
dc.identifier.doi | http://dx.doi.org/10.1107/S174430910900414X | - |
pubs.organisational-data | /Brunel | - |
pubs.organisational-data | /Brunel/Brunel Active Staff | - |
pubs.organisational-data | /Brunel/Brunel Active Staff/School of Health Sciences & Social Care | - |
pubs.organisational-data | /Brunel/Brunel Active Staff/School of Health Sciences & Social Care/Biological Sciences | - |
pubs.organisational-data | /Brunel/Group Publication Pages | - |
pubs.organisational-data | /Brunel/University Research Centres and Groups | - |
pubs.organisational-data | /Brunel/University Research Centres and Groups/School of Health Sciences and Social Care - URCs and Groups | - |
pubs.organisational-data | /Brunel/University Research Centres and Groups/School of Health Sciences and Social Care - URCs and Groups/Centre for Systems and Synthetic Biology | - |
Appears in Collections: | Biological Sciences Publications Dept of Life Sciences Research Papers |
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