Please use this identifier to cite or link to this item:
http://bura.brunel.ac.uk/handle/2438/6645
Title: | The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis |
Authors: | Nichols, CE Sainsbury, S Ren, J Walter, TS Verma, A Stammers, DK Saunders, NJ Owens, RJ |
Keywords: | MarR;Neisseria meningitidis;Transcription factors |
Issue Date: | 2009 |
Publisher: | International Union of Crystallography |
Citation: | Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 65(Pt 3): 204 - 209, Mar 2009 |
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. |
Description: | Copyright @ 2009 Nichols et al. |
URI: | http://onlinelibrary.wiley.com/doi/10.1107/S174430910900414X/abstract http://bura.brunel.ac.uk/handle/2438/6645 |
DOI: | http://dx.doi.org/10.1107/S174430910900414X |
ISSN: | 1744-3091 |
Appears in Collections: | Biological Sciences Publications Dept of Life Sciences Research Papers |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
Fulltext.pdf | 963.19 kB | Adobe PDF | View/Open |
Items in BURA are protected by copyright, with all rights reserved, unless otherwise indicated.