- 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...
Expand abstract - Publication status:
- Published
- 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
- Copyright date:
- 2009
Journal article
The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis.
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