1qlb: Difference between revisions
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[[Image:1qlb.jpg|left|200px]] | [[Image:1qlb.jpg|left|200px]] | ||
'''RESPIRATORY COMPLEX II-LIKE FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES''' | {{Structure | ||
|PDB= 1qlb |SIZE=350|CAPTION= <scene name='initialview01'>1qlb</scene>, resolution 2.33Å | |||
|SITE= <scene name='pdbsite=FA1:Fad+Covalent+Bond+To+Protein+For+Chain+A'>FA1</scene>, <scene name='pdbsite=FA2:Fad+Covalent+Bond+To+Protein+For+Chain+D'>FA2</scene>, <scene name='pdbsite=FS1:Fe4s4+Fe+Sulphur+Centre+Ligands+For+Chain+B'>FS1</scene>, <scene name='pdbsite=FS2:Fe4s4+Fe+Sulphur+Centre+Ligands+For+Chain+E'>FS2</scene>, <scene name='pdbsite=FS3:Fe2s2+Fe+Sulphur+Centre+Ligands+For+Chain+B'>FS3</scene>, <scene name='pdbsite=FS4:Fe2s2+Fe+Sulphur+Centre+Ligands+For+Chain+E'>FS4</scene>, <scene name='pdbsite=FS5:Fe3s4+Fe+Sulphur+Centre+Ligands+For+Chain+B'>FS5</scene>, <scene name='pdbsite=FS6:Fe3s4+Fe+Sulphur+Centre+Ligands+For+Chain+E'>FS6</scene>, <scene name='pdbsite=HE1:Haem+Axial+Ligands+For+Chain+C'>HE1</scene> and <scene name='pdbsite=HE2:Haem+Axial+Ligands+For+Chain+F'>HE2</scene> | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FMR:FUMARATE'>FMR</scene> and <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''RESPIRATORY COMPLEX II-LIKE FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1QLB is a [ | 1QLB is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QLB OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10586875 10586875] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Succinate dehydrogenase]] | [[Category: Succinate dehydrogenase]] | ||
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[[Category: succinate dehydrogenase]] | [[Category: succinate dehydrogenase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:39:10 2008'' | ||
Revision as of 11:39, 20 March 2008
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| 1qlb, resolution 2.33Å | |||||||||||||
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| Sites: | FA1, FA2, FS1, FS2, FS3, FS4, FS5, FS6, HE1 and HE2 | ||||||||||||
| Ligands: | CA, HEM, FES, F3S, SF4, FAD, FMR and LMT | ||||||||||||
| Activity: | Succinate dehydrogenase, with EC number 1.3.99.1 | ||||||||||||
| 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
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