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The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis.


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.

SUBMITTER: Nichols CE 

PROVIDER: S-EPMC2650471 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature

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The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis.

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]

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