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[[Image:1l0l.gif|left|200px]]
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{{STRUCTURE_1l0l|  PDB=1l0l  |  SCENE=  }}
'''structure of bovine mitochondrial cytochrome bc1 complex with a bound fungicide famoxadone'''


==structure of bovine mitochondrial cytochrome bc1 complex with a bound fungicide famoxadone==
<StructureSection load='1l0l' size='340' side='right'caption='[[1l0l]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1l0l]] 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=1L0L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L0L FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</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=FMX:FAMOXADONE'>FMX</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=1l0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l0l OCA], [https://pdbe.org/1l0l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l0l RCSB], [https://www.ebi.ac.uk/pdbsum/1l0l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l0l ProSAT]</span></td></tr>
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l0/1l0l_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1l0l ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1L0L is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L0L OCA].
</div>
<div class="pdbe-citations 1l0l" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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://www.ncbi.nlm.nih.gov/pubmed/12269811 12269811]
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
*[[Cytochrome bc1 3D structures|Cytochrome bc1 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Ubiquinol--cytochrome-c reductase]]
[[Category: Esser L]]
[[Category: Esser, L.]]
[[Category: Gao X]]
[[Category: Gao, X.]]
[[Category: Quinn B]]
[[Category: Quinn, B.]]
[[Category: Tsao S]]
[[Category: Tsao, S.]]
[[Category: Wen X]]
[[Category: Wen, X.]]
[[Category: Xia D]]
[[Category: Xia, D.]]
[[Category: Yu CA]]
[[Category: Yu, C A.]]
[[Category: Yu L]]
[[Category: Yu, L.]]
[[Category: Zhang L]]
[[Category: Zhang, L.]]
[[Category: Cytochrome b]]
[[Category: Cytochrome bc1]]
[[Category: Cytochrome c1]]
[[Category: Heme protein]]
[[Category: Iron sulfur protein]]
[[Category: Membrane protein]]
[[Category: Mitochondrial processing protease]]
[[Category: Mpp]]
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Retrieved from "https://proteopedia.org/1l0l"