The structure of the MarR-family regulator NMB1585 from N. meningitidis has been solved using data extending to 2.1 Å resolution

A. Verma

C.E. Nichols

D.K. Stammers

J. Ren

N.J. Saunders

null null

R.J. Owens

S. Sainsbury

T.S. Walter

Acta Crystallographica Section F Structural Biology and Crystallization Communications

English

PubMed

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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, CE

Sainsbury, S

Ren, J

Walter, TS

Verma, A

Stammers, DK

Saunders, Nigel

Owens, Raymond

Oxford University Research Archive

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

ORA - Oxford University Research Archive

Copyright @ 2009 Nichols et al.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.This work is funded by the UK Medical Research Council and The Biotechnology Biochemical Research Counci

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

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