Open conformation of a flavocytochrome c3 fumarate reductase.
Article Details
- CitationCopy to clipboard
Bamford V, Dobbin PS, Richardson DJ, Hemmings AM
Open conformation of a flavocytochrome c3 fumarate reductase.
Nat Struct Biol. 1999 Dec;6(12):1104-7.
- PubMed ID
- 10581549 [ View in PubMed]
- 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.