1e7p
From Proteopedia
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| - | [[Image:1e7p.gif|left|200px]]<br /> | + | [[Image:1e7p.gif|left|200px]]<br /><applet load="1e7p" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1e7p" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1e7p, resolution 3.10Å" /> | caption="1e7p, resolution 3.10Å" /> | ||
'''QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES'''<br /> | '''QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1E7P 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 NA, HEM, FES, F3S, SF4, FAD, MLA 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] | + | 1E7P 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 NA, HEM, FES, F3S, SF4, FAD, MLA 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] Known structural/functional Sites: <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>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E7P 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 Tue Dec 18 15:02:10 2007'' |
Revision as of 12:52, 18 December 2007
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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 with NA, HEM, FES, F3S, SF4, FAD, MLA and LMT as ligands. Active as Succinate dehydrogenase, with EC number 1.3.99.1 Known structural/functional Sites: , , , , , , , , , , , , , , , , , , and . 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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