1qlb
From Proteopedia
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RESPIRATORY COMPLEX II-LIKE FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES
Overview
Fumarate reductase couples the reduction of fumarate to succinate to the, oxidation of quinol to quinone, in a reaction opposite to that catalysed, by the related complex II of the respiratory chain (succinate, dehydrogenase). Here we describe the crystal structure at 2.2 A resolution, of the three protein subunits containing fumarate reductase from the, anaerobic bacterium Wolinella succinogenes. Subunit A contains the site of, fumarate reduction and a covalently bound flavin adenine dinucleotide, prosthetic group. Subunit B contains three iron-sulphur centres. The, menaquinol-oxidizing subunit C consists of five membrane-spanning, primarily helical segments and binds two haem b molecules. On the basis of, the structure, we propose a pathway of electron transfer from the dihaem, cytochrome b to the site of fumarate reduction and a mechanism of fumarate, reduction. The relative orientations of the soluble and membrane-embedded, subunits of succinate:quinone oxidoreductases appear to be unique.
About this Structure
1QLB is a Protein complex structure of sequences from Wolinella succinogenes with CA, HEM, FES, F3S, SF4, FAD, FMR and LMT as ligands. Active as Succinate dehydrogenase, with EC number 1.3.99.1 Known structural/functional Sites: , , , , , , , , and . Full crystallographic information is available from OCA.
Reference
Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution., Lancaster CR, Kroger A, Auer M, Michel H, Nature. 1999 Nov 25;402(6760):377-85. PMID:10586875
Page seeded by OCA on Tue Dec 18 17:55:51 2007
Categories: Protein complex | Succinate dehydrogenase | Wolinella succinogenes | Auer, M. | Kroeger, A. | Lancaster, C.R.D. | Michel, H. | CA | F3S | FAD | FES | FMR | HEM | LMT | SF4 | Citric acid cycle | Dihaem cytochrome b | Flavoprotein | Fumarate reductase | Iron-sulphur protein | Respiratory chain
