1qo8 | pdb_00001qo8
THE STRUCTURE OF THE OPEN CONFORMATION OF A FLAVOCYTOCHROME C3 FUMARATE REDUCTASE
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| 1qo8, resolution 2.15Å | |||||||||||||
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| Sites: | AC1, AC2, AC3, AC4, AC5, AC6, AC7, AC8, AC9 and BC1 | ||||||||||||
| Ligands: | HEM and FAD | ||||||||||||
| Activity: | Succinate dehydrogenase, with EC number 1.3.99.1 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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