PMID:10581549

Citation	Bamford, V, Dobbin, PS, Richardson, DJ and Hemmings, AM (1999) Open conformation of a flavocytochrome c3 fumarate reductase. Nat. Struct. Biol. 6:1104-7
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.
Links	PubMed Online version:10.1038/70039
Keywords	Amino Acid Sequence; Catalytic Domain; Crystallization; Crystallography, X-Ray; Cytochrome c Group/chemistry; Cytochrome c Group/metabolism; Dimerization; Flavins/metabolism; Fumarates/metabolism; Heme/metabolism; Isoenzymes/chemistry; Isoenzymes/metabolism; Models, Molecular; Molecular Sequence Data; Molecular Weight; Motion; Oxidation-Reduction; Protein Conformation; Shewanella/enzymology; Solubility; Static Electricity; Structure-Activity Relationship; Succinate Dehydrogenase/chemistry; Succinate Dehydrogenase/metabolism
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