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| <StructureSection load='1sqv' size='340' side='right'caption='[[1sqv]], [[Resolution|resolution]] 2.85Å' scene=''> | | <StructureSection load='1sqv' size='340' side='right'caption='[[1sqv]], [[Resolution|resolution]] 2.85Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1sqv]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SQV FirstGlance]. <br> | | <table><tr><td colspan='2'>[[1sqv]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SQV FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=UHD:6-HYDROXY-5-UNDECYL-1,3-BENZOTHIAZOLE-4,7-DIONE'>UHD</scene>, <scene name='pdbligand=UQ2:UBIQUINONE-2'>UQ2</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qcr|1qcr]], [[1lol|1lol]], [[1sqp|1sqp]], [[1sqq|1sqq]], [[1sqb|1sqb]], [[1sqx|1sqx]]</div></td></tr>
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=UHD:6-HYDROXY-5-UNDECYL-1,3-BENZOTHIAZOLE-4,7-DIONE'>UHD</scene>, <scene name='pdbligand=UQ2:UBIQUINONE-2'>UQ2</scene></td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ubiquinol--cytochrome-c_reductase Ubiquinol--cytochrome-c reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.2.2 1.10.2.2] </span></td></tr>
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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sqv OCA], [https://pdbe.org/1sqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sqv RCSB], [https://www.ebi.ac.uk/pdbsum/1sqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sqv ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sqv OCA], [https://pdbe.org/1sqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sqv RCSB], [https://www.ebi.ac.uk/pdbsum/1sqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sqv ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[https://www.uniprot.org/uniprot/QCR10_BOVIN QCR10_BOVIN]] This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may be closely linked to the iron-sulfur protein in the complex and function as an iron-sulfur protein binding factor. [[https://www.uniprot.org/uniprot/CYB_BOVIN CYB_BOVIN]] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. [[https://www.uniprot.org/uniprot/UCRI_BOVIN UCRI_BOVIN]] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The transit peptide of the Rieske protein seems to form part of the bc1 complex and is considered to be the subunit 11/IX of that complex. [[https://www.uniprot.org/uniprot/QCR2_BOVIN QCR2_BOVIN]] This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. The core protein 2 is required for the assembly of the complex. [[https://www.uniprot.org/uniprot/QCR6_BOVIN QCR6_BOVIN]] This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may mediate formation of the complex between cytochromes c and c1. [[https://www.uniprot.org/uniprot/QCR1_BOVIN QCR1_BOVIN]] This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may mediate formation of the complex between cytochromes c and c1. [[https://www.uniprot.org/uniprot/CY1_BOVIN CY1_BOVIN]] This is the heme-containing component of the cytochrome b-c1 complex, which accepts electrons from Rieske protein and transfers electrons to cytochrome c in the mitochondrial respiratory chain. [[https://www.uniprot.org/uniprot/QCR9_BOVIN QCR9_BOVIN]] This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This subunit interacts with cytochrome c1.
| | [https://www.uniprot.org/uniprot/QCR1_BOVIN QCR1_BOVIN] This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may mediate formation of the complex between cytochromes c and c1. |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1sqv ConSurf]. | | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1sqv ConSurf]. |
| <div style="clear:both"></div> | | <div style="clear:both"></div> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Cytochrome bc(1) is an integral membrane protein complex essential for cellular respiration and photosynthesis; it couples electron transfer from quinol to cytochrome c to proton translocation across the membrane. Specific bc(1) inhibitors have not only played crucial roles in elucidating the mechanism of bc(1) function but have also provided leads for the development of novel antibiotics. Crystal structures of bovine bc(1) in complex with the specific Q(o) site inhibitors azoxystrobin, MOAS, myxothiazol, stigmatellin and 5-undecyl-6-hydroxy-4,7-dioxobenzothiazole were determined. Interactions, conformational changes and possible mechanisms of resistance, specific to each inhibitor, were defined. Residues and secondary structure elements that are capable of discriminating different classes of Q(o) site inhibitors were identified for the cytochrome b subunit. Directions in the displacement of the cd1 helix of cytochrome b subunit in response to various Q(o) site inhibitors were correlated to the binary conformational switch of the extrinsic domain of the iron-sulfur protein subunit. The new structural information, together with structures previously determined, provide a basis that, combined with biophysical and mutational data, suggest a modification to the existing classification of bc(1) inhibitors. bc(1) inhibitors are grouped into three classes: class P inhibitors bind to the Q(o) site, class N inhibitors bind to the Q(i) site and the class PN inhibitors target both sites. Class P contains two subgroups, Pm and Pf, that are distinct by their ability to induce mobile or fixed conformation of iron-sulfur protein.
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| Crystallographic studies of quinol oxidation site inhibitors: a modified classification of inhibitors for the cytochrome bc(1) complex.,Esser L, Quinn B, Li YF, Zhang M, Elberry M, Yu L, Yu CA, Xia D J Mol Biol. 2004 Jul 30;341(1):281-302. PMID:15312779<ref>PMID:15312779</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 1sqv" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Cytochrome C 3D structures|Cytochrome C 3D structures]] | | *[[Cytochrome C 3D structures|Cytochrome C 3D structures]] |
| *[[Cytochrome bc1 complex|Cytochrome bc1 complex]] | | *[[Cytochrome bc1 3D structures|Cytochrome bc1 3D structures]] |
| == References ==
| |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Bos taurus]] | | [[Category: Bos taurus]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Ubiquinol--cytochrome-c reductase]]
| | [[Category: Elberry M]] |
| [[Category: Elberry, M]] | | [[Category: Esser L]] |
| [[Category: Esser, L]] | | [[Category: Li YF]] |
| [[Category: Li, Y F]] | | [[Category: Quinn B]] |
| [[Category: Quinn, B]] | | [[Category: Xia D]] |
| [[Category: Xia, D]] | | [[Category: Yu CA]] |
| [[Category: Yu, C A]] | | [[Category: Yu L]] |
| [[Category: Yu, L]] | | [[Category: Zhang M]] |
| [[Category: Zhang, M]] | |
| [[Category: Cytochrome bc1]]
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| [[Category: Electron transport]]
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| [[Category: Membrane protein]]
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| [[Category: Oxidoreductase]]
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| [[Category: Qo inhibitor]]
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