1qo8: Difference between revisions
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==Overview== | ==Overview== | ||
Fumarate reductases and succinate dehydrogenases play central roles in the | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Succinate dehydrogenase]] | [[Category: Succinate dehydrogenase]] | ||
[[Category: Bamford, V.]] | [[Category: Bamford, V.]] | ||
[[Category: Dobbin, P | [[Category: Dobbin, P S.]] | ||
[[Category: Hemmings, A | [[Category: Hemmings, A M.]] | ||
[[Category: Richardson, D | [[Category: Richardson, D J.]] | ||
[[Category: FAD]] | [[Category: FAD]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:41:52 2008'' | ||
Revision as of 12:41, 21 February 2008
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THE STRUCTURE OF THE OPEN CONFORMATION OF A FLAVOCYTOCHROME C3 FUMARATE REDUCTASE
Overview
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.
About this Structure
1QO8 is a Single protein structure of sequence from Shewanella frigidimarina with HEM and FAD as ligands. Active as Succinate dehydrogenase, with EC number 1.3.99.1 Known structural/functional Sites: AC1, AC2, AC3, AC4, AC5, AC6, AC7, AC8, AC9 and BC1. Full crystallographic information is available from OCA.
Reference
Open conformation of a flavocytochrome c3 fumarate reductase., Bamford V, Dobbin PS, Richardson DJ, Hemmings AM, Nat Struct Biol. 1999 Dec;6(12):1104-7. PMID:10581549
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