Open conformation of a flavocytochrome c3 fumarate reductase.
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.
Bamford
V
V
School of Biological Sciences, Centre for Metalloprotein Spectroscopy and Biology, University of East Anglia, Norwich NR4 7TJ, UK.
Dobbin
P S
PS
Richardson
D J
DJ
Hemmings
A M
AM
D000595:Amino Acid Sequence; D020134:Catalytic Domain; D003460:Crystallization; D018360:Crystallography, X-Ray; D003574:Cytochrome c Group / Q000737:chemistry* / Q000378:metabolism*; D019281:Dimerization; D005415:Flavins / Q000378:metabolism; D005650:Fumarates / Q000378:metabolism; D006418:Heme / Q000378:metabolism; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009038:Motion; D010084:Oxidation-Reduction; D011487:Protein Conformation; D020592:Shewanella / Q000201:enzymology*; D012995:Solubility; D055672:Static Electricity; D013329:Structure-Activity Relationship; D013385:Succinate Dehydrogenase / Q000737:chemistry* / Q000378:metabolism*
D003574:Cytochrome c Group; D005415:Flavins; D005650:Fumarates; D007527:Isoenzymes; D006418:Heme; C032005:fumaric acid; C112400:flavocytochrome c3; D013385:Succinate Dehydrogenase