Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 65, Issue -, Pages 204-209Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S174430910900414X
Keywords
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Funding
- UK Medical Research Council
- The Biotechnology Biochemical Research Council
- MRC [G0500367, G0701506] Funding Source: UKRI
- Medical Research Council [G0701506, G0500367] Funding Source: researchfish
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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 angstrom. 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.
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