1qlb
From Proteopedia
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==Overview== | ==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, . | + | 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== | ||
| - | 1QLB is a | + | 1QLB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes] with CA, HEM, FES, F3S, SF4, FAD, FMR and LMT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] Structure known Active Sites: FA1, FA2, FS1, FS2, FS3, FS4, FS5, FS6, HE1 and HE2. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QLB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: succinate dehydrogenase]] | [[Category: succinate dehydrogenase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:39:29 2007'' |
Revision as of 12:34, 5 November 2007
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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 Structure known Active 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
Page seeded by OCA on Mon Nov 5 14:39:29 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
