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

Journal article

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: Nichols, C; Sainsbury, S; Ren, J; Walter, T; Verma, A

• Publication status: Published
• Journal: Acta crystallographica. Section F, Structural biology and crystallization communications
• Volume: 65
• Issue: Pt 3
• Pages: 204-209
• Publication date: 2009-03-01
• DOI: 10.1107/s174430910900414x
• EISSN: 1744-3091
• ISSN: 1744-3091
• Language: English
• Keywords: Binding Sites; Escherichia coli; Models, Molecular; Crystallography, X-Ray; DNA, Bacterial; Protein Binding; Amino Acid Sequence; Molecular Sequence Data; Neisseria meningitidis; Bacterial Proteins; Sequence Alignment