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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 i...

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Publication status:
Published

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Publisher copy:
10.1107/s174430910900414x

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Journal:
Acta crystallographica. Section F, Structural biology and crystallization communications
Volume:
65
Issue:
Pt 3
Pages:
204-209
Publication date:
2009-03-05
DOI:
EISSN:
1744-3091
ISSN:
1744-3091
URN:
uuid:3d901465-655b-4694-8769-c89b9e16107f
Source identifiers:
23610
Local pid:
pubs:23610

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