title: The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis.
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 A. Overall, the dimeric structure resembles those of other MarR proteins, with each subunit comprising a winged helix-turn-helix (wHtH) domain connected to an alpha-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.
authors.affiliation: Wellcome Trust Centre for Human Genetics, University of Oxford, England.
authors.forename: Charles E
authors.initials: CE
authors.lastname: Nichols
authors.forename: Sarah
authors.initials: S
authors.lastname: Sainsbury
authors.forename: Jingshan
authors.initials: J
authors.lastname: Ren
authors.forename: Thomas S
authors.initials: TS
authors.lastname: Walter
authors.forename: Anil
authors.initials: A
authors.lastname: Verma
authors.forename: David K
authors.initials: DK
authors.lastname: Stammers
authors.forename: Nigel J
authors.initials: NJ
authors.lastname: Saunders
authors.forename: Raymond J
authors.initials: RJ
authors.lastname: Owens
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D018360:Crystallography, X-Ray; D004269:DNA, Bacterial / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009345:Neisseria meningitidis / Q000737:chemistry*; D011485:Protein Binding; D016415:Sequence Alignment
chemical_list: D001426:Bacterial Proteins; D004269:DNA, Bacterial