Structural highlights
Function
[FRD2_SHEFN] Catalyzes unidirectional fumarate reduction using artificial electron donors such as methyl viologen. The physiological reductant is unknown.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. PMID:10581549 doi:http://dx.doi.org/10.1038/70039
