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1opc
From Proteopedia
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[[Category: winged helix]] | [[Category: winged helix]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:58:14 2007'' |
Revision as of 13:53, 30 October 2007
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OMPR DNA-BINDING DOMAIN, ESCHERICHIA COLI
Overview
BACKGROUND: The differential expression of the ompF and ompC genes is, regulated by two proteins that belong to the two component family of, signal transduction proteins: the histidine kinase, EnvZ, and the response, regulator, OmpR. OmpR belongs to a subfamily of at least 50 response, regulators with homologous C-terminal DNA-binding domains of approximately, 98 amino acids. Sequence homology with DNA-binding proteins of known, structure cannot be detected, and the lack of structural information has, prevented understanding of many of this familys functional properties., RESULTS: We have determined the crystal structure of the Escherichia coli, OmpR C-terminal domain at 1.95 A resolution. The structure consists of, three alpha helices packed against two antiparallel beta sheets. Two, ... [(full description)]
About this Structure
1OPC is a [Single protein] structure of sequence from [Escherichia coli]. Structure known Active Sites: ALP, RH and W1. Full crystallographic information is available from [OCA].
Reference
The DNA-binding domain of OmpR: crystal structures of a winged helix transcription factor., Martinez-Hackert E, Stock AM, Structure. 1997 Jan 15;5(1):109-24. PMID:9016718
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