Open AccessThe structure of NMB1585, a MarR‐family regulator from Neisseria meningitidis
Author(s) -
Nichols Charles E.,
Sainsbury Sarah,
Ren Jingshan,
Walter Thomas S.,
Verma Anil,
Stammers David K.,
Saunders Nigel J.,
Owens Raymond J.
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910900414x
Subject(s) - repressor , neisseria meningitidis , inducer , protein subunit , helix (gastropod) , chemistry , transcription (linguistics) , promoter , regulator , resolution (logic) , neisseria , dna , domain (mathematical analysis) , biology , stereochemistry , transcription factor , genetics , gene , gene expression , bacteria , linguistics , philosophy , mathematics , artificial intelligence , snail , computer science , ecology , mathematical analysis
The structure of the MarR‐family transcription factor NMB1585 from Neisseria meningitidis has been solved using data extending to a resolution of 2.1 Å. Overall, the dimeric structure resembles those of other MarR proteins, with each subunit comprising a winged helix–turn–helix (wHtH) domain connected to an α‐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.