1e7p
From Proteopedia
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|PDB= 1e7p |SIZE=350|CAPTION= <scene name='initialview01'>1e7p</scene>, resolution 3.10Å | |PDB= 1e7p |SIZE=350|CAPTION= <scene name='initialview01'>1e7p</scene>, resolution 3.10Å | ||
|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=FA3:Fad+Covalent+Bond+To+Protein+For+Chain+G'>FA3</scene>, <scene name='pdbsite=FA4:Fad+Covalent+Bond+To+Protein+For+Chain+K'>FA4</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=FS7:Fe4s4+Fe+Sulphur+Centre+Ligands+For+Chain+G'>FS7</scene>, <scene name='pdbsite=FS8:Fe4s4+Fe+Sulphur+Centre+Ligands+For+Chain+K'>FS8</scene>, <scene name='pdbsite=FS9:Fe2s2+Fe+Sulphur+Centre+Ligands+For+Chain+G'>FS9</scene>, <scene name='pdbsite=FSA:Fe2s2+Fe+Sulphur+Centre+Ligands+For+Chain+K'>FSA</scene>, <scene name='pdbsite=FSB:Fe3s4+Fe+Sulphur+Centre+Ligands+For+Chain+G'>FSB</scene>, <scene name='pdbsite=FSC:Fe3s4+Fe+Sulphur+Centre+Ligands+For+Chain+K'>FSC</scene>, <scene name='pdbsite=HE1:Haem+Axial+Ligands+For+Chain+C'>HE1</scene>, <scene name='pdbsite=HE2:Haem+Axial+Ligands+For+Chain+F'>HE2</scene>, <scene name='pdbsite=HE3:Haem+Axial+Ligands+For+Chain+I'>HE3</scene> and <scene name='pdbsite=HE4:Haem+Axial+Ligands+For+Chain+L'>HE4</scene> | |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=FA3:Fad+Covalent+Bond+To+Protein+For+Chain+G'>FA3</scene>, <scene name='pdbsite=FA4:Fad+Covalent+Bond+To+Protein+For+Chain+K'>FA4</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=FS7:Fe4s4+Fe+Sulphur+Centre+Ligands+For+Chain+G'>FS7</scene>, <scene name='pdbsite=FS8:Fe4s4+Fe+Sulphur+Centre+Ligands+For+Chain+K'>FS8</scene>, <scene name='pdbsite=FS9:Fe2s2+Fe+Sulphur+Centre+Ligands+For+Chain+G'>FS9</scene>, <scene name='pdbsite=FSA:Fe2s2+Fe+Sulphur+Centre+Ligands+For+Chain+K'>FSA</scene>, <scene name='pdbsite=FSB:Fe3s4+Fe+Sulphur+Centre+Ligands+For+Chain+G'>FSB</scene>, <scene name='pdbsite=FSC:Fe3s4+Fe+Sulphur+Centre+Ligands+For+Chain+K'>FSC</scene>, <scene name='pdbsite=HE1:Haem+Axial+Ligands+For+Chain+C'>HE1</scene>, <scene name='pdbsite=HE2:Haem+Axial+Ligands+For+Chain+F'>HE2</scene>, <scene name='pdbsite=HE3:Haem+Axial+Ligands+For+Chain+I'>HE3</scene> and <scene name='pdbsite=HE4:Haem+Axial+Ligands+For+Chain+L'>HE4</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e7p OCA], [http://www.ebi.ac.uk/pdbsum/1e7p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e7p RCSB]</span> | ||
}} | }} | ||
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[[Category: Wolinella succinogenes]] | [[Category: Wolinella succinogenes]] | ||
[[Category: Lancaster, C R.D.]] | [[Category: Lancaster, C R.D.]] | ||
| - | [[Category: F3S]] | ||
| - | [[Category: FAD]] | ||
| - | [[Category: FES]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: LMT]] | ||
| - | [[Category: MLA]] | ||
| - | [[Category: NA]] | ||
| - | [[Category: SF4]] | ||
[[Category: citric acid cycle]] | [[Category: citric acid cycle]] | ||
[[Category: dihaem cytochrome b]] | [[Category: dihaem cytochrome b]] | ||
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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 Sun Mar 30 19:56:55 2008'' |
Revision as of 16:56, 30 March 2008
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| , resolution 3.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , , , , , , , , , , , , and | ||||||
| Ligands: | , , , , , , , | ||||||
| Activity: | Succinate dehydrogenase, with EC number 1.3.99.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES
Overview
Quinol:fumarate reductase (QFR) is a membrane protein complex that couples the reduction of fumarate to succinate to the oxidation of quinol to quinone. Previously, the crystal structure of QFR from Wolinella succinogenes was determined based on two different crystal forms, and the site of fumarate binding in the flavoprotein subunit A of the enzyme was located between the FAD-binding domain and the capping domain [Lancaster, C.R.D., Kroger, A., Auer, M., & Michel, H. (1999) Nature 402, 377--385]. Here we describe the structure of W. succinogenes QFR based on a third crystal form and refined at 3.1 A resolution. Compared with the previous crystal forms, the capping domain is rotated in this structure by approximately 14 degrees relative to the FAD-binding domain. As a consequence, the topology of the dicarboxylate binding site is much more similar to those of membrane-bound and soluble fumarate reductase enzymes from other organisms than to that found in the previous crystal forms of W. succinogenes QFR. This and the effects of the replacement of Arg A301 by Glu or Lys by site-directed mutagenesis strongly support a common mechanism for fumarate reduction in this superfamily of enzymes.
About this Structure
1E7P is a Protein complex structure of sequences from Wolinella succinogenes. Full crystallographic information is available from OCA.
Reference
A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction., Lancaster CR, Gross R, Simon J, Eur J Biochem. 2001 Mar;268(6):1820-7. PMID:11248702
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