1l0n

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[[Image:1l0n.gif|left|200px]]<br /><applet load="1l0n" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1l0n, resolution 2.60&Aring;" />
 
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'''native structure of bovine mitochondrial cytochrome bc1 complex'''<br />
 
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==Overview==
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==native structure of bovine mitochondrial cytochrome bc1 complex==
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<StructureSection load='1l0n' size='340' side='right'caption='[[1l0n]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1l0n]] 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=1L0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L0N FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=1l0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l0n OCA], [https://pdbe.org/1l0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l0n RCSB], [https://www.ebi.ac.uk/pdbsum/1l0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l0n ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l0/1l0n_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1l0n ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
Ubiquinol cytochrome c oxido-reductase (EC. 1.10.2.2, bc1) is an integral membrane protein complex essential to cellular respiration. Structures of the 11-subunit mitochondrial bc1 complex were determined with and without the fungicide famoxadone. Specific inhibition by famoxadone is achieved through a coordinated optimization of aromatic-aromatic interactions where conformational rearrangements in famoxadone and in residues lining the inhibitor-binding pocket produce a network of aromatic-aromatic interactions that mimic the crystal lattice of benzene. The profound aromatic-aromatic interactions as supported by prior mutagenesis provide a structural basis for specific protein-ligand interaction in a hydrophobic environment. Dramatic conformational changes, both in cyt. b and ISP subunits in the inhibitor-protein complex, confer experimental evidence for a functional role of cytochrome b in the induced conformational arrest of ISP and allow the identification of a possible intrasubunit signal transduction pathway that controls the movement of ISP. These results support an inhibitory mechanism that is consistent with the requirement for ISP movement in the electron transfer of this complex.
Ubiquinol cytochrome c oxido-reductase (EC. 1.10.2.2, bc1) is an integral membrane protein complex essential to cellular respiration. Structures of the 11-subunit mitochondrial bc1 complex were determined with and without the fungicide famoxadone. Specific inhibition by famoxadone is achieved through a coordinated optimization of aromatic-aromatic interactions where conformational rearrangements in famoxadone and in residues lining the inhibitor-binding pocket produce a network of aromatic-aromatic interactions that mimic the crystal lattice of benzene. The profound aromatic-aromatic interactions as supported by prior mutagenesis provide a structural basis for specific protein-ligand interaction in a hydrophobic environment. Dramatic conformational changes, both in cyt. b and ISP subunits in the inhibitor-protein complex, confer experimental evidence for a functional role of cytochrome b in the induced conformational arrest of ISP and allow the identification of a possible intrasubunit signal transduction pathway that controls the movement of ISP. These results support an inhibitory mechanism that is consistent with the requirement for ISP movement in the electron transfer of this complex.
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==About this Structure==
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The crystal structure of mitochondrial cytochrome bc1 in complex with famoxadone: the role of aromatic-aromatic interaction in inhibition.,Gao X, Wen X, Yu C, Esser L, Tsao S, Quinn B, Zhang L, Yu L, Xia D Biochemistry. 2002 Oct 1;41(39):11692-702. PMID:12269811<ref>PMID:12269811</ref>
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1L0N is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=FES:'>FES</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ubiquinol--cytochrome-c_reductase Ubiquinol--cytochrome-c reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.2.2 1.10.2.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L0N OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The crystal structure of mitochondrial cytochrome bc1 in complex with famoxadone: the role of aromatic-aromatic interaction in inhibition., Gao X, Wen X, Yu C, Esser L, Tsao S, Quinn B, Zhang L, Yu L, Xia D, Biochemistry. 2002 Oct 1;41(39):11692-702. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12269811 12269811]
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</div>
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[[Category: Bos taurus]]
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<div class="pdbe-citations 1l0n" style="background-color:#fffaf0;"></div>
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[[Category: Protein complex]]
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[[Category: Ubiquinol--cytochrome-c reductase]]
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[[Category: Esser, L.]]
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[[Category: Gao, X.]]
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[[Category: Quinn, B.]]
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[[Category: Tsao, S.]]
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[[Category: Wen, X.]]
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[[Category: Xia, D.]]
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[[Category: Yu, C A.]]
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[[Category: Yu, L.]]
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[[Category: Zhang, L.]]
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[[Category: FES]]
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[[Category: HEM]]
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[[Category: cytochrome b]]
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[[Category: cytochrome bc1]]
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[[Category: cytochrome c1]]
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[[Category: heme protein]]
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[[Category: iron sulfur protein]]
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[[Category: membrane protein]]
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[[Category: mitochondrial processing protease]]
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[[Category: mpp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:39:59 2008''
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==See Also==
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*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
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*[[Cytochrome bc1 3D structures|Cytochrome bc1 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bos taurus]]
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[[Category: Large Structures]]
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[[Category: Esser L]]
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[[Category: Gao X]]
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[[Category: Quinn B]]
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[[Category: Tsao S]]
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[[Category: Wen X]]
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[[Category: Xia D]]
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[[Category: Yu CA]]
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[[Category: Yu L]]
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[[Category: Zhang L]]

Current revision

native structure of bovine mitochondrial cytochrome bc1 complex

PDB ID 1l0n

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