1QLB

respiratory complex II-like fumarate reductase from Wolinella succinogenes

Summary for 1QLB

• Entry DOI: 10.2210/pdb1qlb/pdb
• Related: 1FUM 1QLA
• Descriptor: FUMARATE REDUCTASE FLAVOPROTEIN SUBUNIT, PROTOPORPHYRIN IX CONTAINING FE, DODECYL-BETA-D-MALTOSIDE, ... (12 entities in total)
• Functional Keywords: oxidoreductase, citric acid cycle, respiratory chain iron-sulphur protein
• Biological source: WOLINELLA SUCCINOGENES; More
• Cellular location: Cell membrane; Multi-pass membrane protein: P17413
• Total number of polymer chains: 6
• Total formula weight: 266812.50

Authors

Lancaster, C.R.D.,Kroeger, A.,Auer, M.,Michel, H. (deposition date: 1999-08-25, release date: 1999-11-29, Last modification date: 2024-11-13)

Primary citation

Lancaster, C.R.D.,Kroeger, A.,Auer, M.,Michel, H.
Structure of Fumarate Reductase from Wolinella Succinogenes at 2.2 Angstroms Resolution
Nature, 402:377-, 1999

PubMed Abstract: 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.

PubMed: 10586875
DOI: 10.1038/46483

Experimental method

X-RAY DIFFRACTION (2.33 Å)