Please use this identifier to cite or link to this item: http://buratest.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

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