Ontology highlight
ABSTRACT:
SUBMITTER: Nichols CE
PROVIDER: S-EPMC2650471 | biostudies-literature | 2009 Mar
REPOSITORIES: biostudies-literature
Nichols Charles E CE 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
Acta crystallographica. Section F, Structural biology and crystallization communications 20090226 Pt 3
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 l ...[more]