1qlb: Difference between revisions
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==Overview== | ==Overview== | ||
Fumarate reductase couples the reduction of fumarate to succinate to the | 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== | ==About this Structure== | ||
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[[Category: Auer, M.]] | [[Category: Auer, M.]] | ||
[[Category: Kroeger, A.]] | [[Category: Kroeger, A.]] | ||
[[Category: Lancaster, C | [[Category: Lancaster, C R.D.]] | ||
[[Category: Michel, H.]] | [[Category: Michel, H.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: succinate dehydrogenase]] | [[Category: succinate dehydrogenase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:40:57 2008'' | ||
Revision as of 12:40, 21 February 2008
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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: FA1, FA2, FS1, FS2, FS3, FS4, FS5, FS6, HE1 and HE2. 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
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