1qlb
From Proteopedia
| |||||||
| , resolution 2.33Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , , and | ||||||
| Ligands: | , , , , , , , | ||||||
| Activity: | Succinate dehydrogenase, with EC number 1.3.99.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Sun Mar 30 23:15:20 2008
