1qo8
From Proteopedia
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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 and as ligands. Active as Succinate dehydrogenase, with EC number 1.3.99.1 Known structural/functional Sites: , , , , , , , , and . 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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