3bcc

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{{STRUCTURE_3bcc| PDB=3bcc | SCENE= }}
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==STIGMATELLIN AND ANTIMYCIN BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN==
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===STIGMATELLIN AND ANTIMYCIN BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN===
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<StructureSection load='3bcc' size='340' side='right' caption='[[3bcc]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
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{{ABSTRACT_PUBMED_9565029}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3bcc]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BCC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BCC FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMY:ANTIMYCIN'>AMY</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SIG:STIGMATELLIN'>SIG</scene><br>
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<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bcc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3bcc RCSB], [http://www.ebi.ac.uk/pdbsum/3bcc PDBsum]</span></td></tr>
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<table>
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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/bc/3bcc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata 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 ==
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The cytochrome bc1 is one of the three major respiratory enzyme complexes residing in the inner mitochondrial membrane. Cytochrome bc1 transfers electrons from ubiquinol to cytochrome c and uses the energy thus released to form an electrochemical gradient across the inner membrane. Our X-ray crystal structures of the complex from chicken, cow and rabbit in both the presence and absence of inhibitors of quinone oxidation, reveal two different locations for the extrinsic domain of one component of the enzyme, an iron-sulphur protein. One location is close enough to the supposed quinol oxidation site to allow reduction of the Fe-S protein by ubiquinol. The other site is close enough to cytochrome c1 to allow oxidation of the Fe-S protein by the cytochrome. As neither location will allow both reactions to proceed at a suitable rate, the reaction mechanism must involve movement of the extrinsic domain of the Fe-S component in order to shuttle electrons from ubiquinol to cytochrome c1. Such a mechanism has not previously been observed in redox protein complexes.
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==Function==
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Electron transfer by domain movement in cytochrome bc1.,Zhang Z, Huang L, Shulmeister VM, Chi YI, Kim KK, Hung LW, Crofts AR, Berry EA, Kim SH Nature. 1998 Apr 16;392(6677):677-84. PMID:9565029<ref>PMID:9565029</ref>
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[[http://www.uniprot.org/uniprot/CYB_CHICK CYB_CHICK]] 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 (By similarity). [[http://www.uniprot.org/uniprot/UCRH_BOVIN UCRH_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. [[http://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. [[http://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.
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==About this Structure==
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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[[3bcc]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BCC OCA].
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</div>
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== References ==
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==See Also==
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<references/>
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*[[Cytochrome bc1 complex|Cytochrome bc1 complex]]
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__TOC__
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*[[Cytochrome c|Cytochrome c]]
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</StructureSection>
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[[Category: Chick]]
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==Reference==
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<ref group="xtra">PMID:009565029</ref><ref group="xtra">PMID:010468555</ref><references group="xtra"/><references/>
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[[Category: Gallus gallus]]
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[[Category: Ubiquinol--cytochrome-c reductase]]
[[Category: Ubiquinol--cytochrome-c reductase]]
[[Category: Berry, E A.]]
[[Category: Berry, E A.]]

Revision as of 06:58, 28 May 2014

STIGMATELLIN AND ANTIMYCIN BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN

3bcc, resolution 3.70Å

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