1QO8

The structure of the open conformation of a flavocytochrome c3 fumarate reductase

Summary for 1QO8

Entry DOI	10.2210/pdb1qo8/pdb
Descriptor	FLAVOCYTOCHROME C3 FUMARATE REDUCTASE, PROTOPORPHYRIN IX CONTAINING FE, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
Functional Keywords	oxidoreductase
Biological source	SHEWANELLA FRIGIDIMARINA
Total number of polymer chains	2
Total formula weight	128031.96
Authors	Bamford, V.,Dobbin, P.S.,Richardson, D.J.,Hemmings, A.M. (deposition date: 1999-11-04, release date: 2000-11-02, Last modification date: 2024-05-08)
Primary citation	Bamford, V.,Dobbin, P.S.,Richardson, D.J.,Hemmings, A.M. Open Conformation of a Flavocytochrome C3 Fumarate Reductase. Nat.Struct.Biol., 6:1104-, 1999 Cited by 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. PubMed: 10581549 DOI: 10.1038/70039 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.15 Å)

Structure validation