The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 65; no. 3; pp. 204 - 209
• Main Authors: Nichols, Charles E., Sainsbury, Sarah, Ren, Jingshan, Walter, Thomas S., Verma, Anil, Stammers, David K., Saunders, Nigel J., Owens, Raymond J.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.03.2009
• Subjects: Amino Acid Sequence; Bacterial Proteins - chemistry; Binding Sites; Crystallography, X-Ray; DNA, Bacterial - metabolism; Escherichia coli - chemistry; MarR; Models, Molecular; Molecular Sequence Data; Neisseria meningitidis; Neisseria meningitidis - chemistry; Protein Binding; Sequence Alignment; Structural Communications; transcription factors
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S174430910900414X

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.