The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis.
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.
Nichols
Charles E
CE
Wellcome Trust Centre for Human Genetics, University of Oxford, England.
Sainsbury
Sarah
S
Ren
Jingshan
J
Walter
Thomas S
TS
Verma
Anil
A
Stammers
David K
DK
Saunders
Nigel J
NJ
Owens
Raymond J
RJ
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D018360:Crystallography, X-Ray; D004269:DNA, Bacterial / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009345:Neisseria meningitidis / Q000737:chemistry*; D011485:Protein Binding; D016415:Sequence Alignment
D001426:Bacterial Proteins; D004269:DNA, Bacterial