Download MendeleyThe structure of NMB1585, a MarR-family regulator from Neisseria meningitidis
Nichols, C.E., Sainsbury, S., Ren, J., Walter, T.S., Verma, A., Stammers, D.K., Saunders, N.J., Owens, R.J.(2009) Acta Crystallogr Sect F Struct Biol Cryst Commun 65: 204-209
- PubMed: 19255465
- DOI: https://doi.org/10.1107/S174430910900414X
- Primary Citation of Related Structures:
3G3Z - PubMed 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.
Organizational Affiliation:
Wellcome Trust Centre for Human Genetics, University of Oxford, England.
