3G3Z
The structure of NMB1585, a MarR family regulator from Neisseria meningitidis
Summary for 3G3Z
| Entry DOI | 10.2210/pdb3g3z/pdb |
| Descriptor | Transcriptional regulator, MarR family (2 entities in total) |
| Functional Keywords | marr, neisseria meningitidis, transcription factor, structural genomics, oxford protein production facility, oppf, transcription |
| Biological source | Neisseria meningitidis serogroup B |
| Total number of polymer chains | 2 |
| Total formula weight | 32858.56 |
| Authors | Nichols, C.E.,Sainsbury, S.,Ren, J.,Walter, T.S.,Verma, A.,Stammers, D.K.,Saunders, N.J.,Owens, R.J.,Oxford Protein Production Facility (OPPF) (deposition date: 2009-02-03, release date: 2009-04-14, Last modification date: 2024-10-30) |
| Primary citation | Nichols, C.E.,Sainsbury, S.,Ren, J.,Walter, T.S.,Verma, A.,Stammers, D.K.,Saunders, N.J.,Owens, R.J. The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis Acta Crystallogr.,Sect.F, 65:204-209, 2009 Cited by 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. PubMed: 19255465DOI: 10.1107/S174430910900414X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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