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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.

Original publication

DOI

10.1107/S174430910900414X

Type

Journal article

Journal

Acta Crystallogr Sect F Struct Biol Cryst Commun

Publication Date

01/03/2009

Volume

65

Pages

204 - 209

Keywords

Amino Acid Sequence, Bacterial Proteins, Binding Sites, Crystallography, X-Ray, DNA, Bacterial, Escherichia coli, Models, Molecular, Molecular Sequence Data, Neisseria meningitidis, Protein Binding, Sequence Alignment