Open conformation of a flavocytochrome c3 fumarate reductase

Bamford, Vicki, Dobbin, Paul S., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Hemmings, Andrew M. ORCID: https://orcid.org/0000-0003-3053-3134 (1999) Open conformation of a flavocytochrome c3 fumarate reductase. Nature Structural Biology, 6 (12). pp. 1104-1107. ISSN 1072-8368

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Abstract

Fumarate reductases and succinate dehydrogenases play central roles in the metabolism of eukaryotic and prokaryotic cells. A recent medium resolution structure of the Escherichia coli fumarate reductase (Frd) has revealed the overall organization of the membrane-bound complex. Here we present the first high resolution X-ray crystal structure of a water-soluble bacterial fumarate reductase in an open conformation. This structure reveals a mobile domain that modulates substrate access to the active site and provides new insights into the mechanism of this widespread and important family of FAD-containing respiratory proteins.

Item Type: Article
Additional Information: Funding Information: We would like to acknowledge the support of the Wellcome Trust to P.S.D. and D.J.R. We are grateful also for access to the facilities of the BM14 beamline at the ESRF, the EMBL BW7B beamline at the Doris storage ring, DESY, Hamburg, and the UEA Centre for Metalloprotein Spectroscopy and Biology (CMSB).
Uncontrolled Keywords: structural biology,biochemistry,genetics ,/dk/atira/pure/subjectarea/asjc/1300/1315
Faculty \ School:
Faculty of Science > School of Biological Sciences
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Depositing User: LivePure Connector
Date Deposited: 15 Jul 2022 12:30
Last Modified: 12 Aug 2022 05:36
URI: https://ueaeprints.uea.ac.uk/id/eprint/86195
DOI: 10.1038/70039

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