Reference: Bamford V, et al. (1999) Open conformation of a flavocytochrome c3 fumarate reductase. Nat Struct Biol 6(12):1104-7

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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.

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Journal Article | Research Support, Non-U.S. Gov't
Authors
Bamford V, Dobbin PS, Richardson DJ, Hemmings AM
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