2bcc

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[[Image:2bcc.gif|left|200px]]
 
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==STIGMATELLIN-BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN==
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The line below this paragraph, containing "STRUCTURE_2bcc", creates the "Structure Box" on the page.
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<StructureSection load='2bcc' size='340' side='right'caption='[[2bcc]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2bcc]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BCC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BCC FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 3.5&#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=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PEE:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>PEE</scene>, <scene name='pdbligand=SIG:STIGMATELLIN'>SIG</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</scene></td></tr>
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{{STRUCTURE_2bcc| PDB=2bcc | SCENE= }}
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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=2bcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bcc OCA], [https://pdbe.org/2bcc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bcc RCSB], [https://www.ebi.ac.uk/pdbsum/2bcc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bcc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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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/2bcc_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/main_output.php?pdb_ID=2bcc 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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'''STIGMATELLIN-BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN'''
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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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==Overview==
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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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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2BCC is a [[Single protein]] structure of 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=2BCC OCA].
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</div>
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<div class="pdbe-citations 2bcc" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9565029 9565029]
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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>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Ubiquinol--cytochrome-c reductase]]
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[[Category: Berry EA]]
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[[Category: Berry, E A.]]
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[[Category: Chi YI]]
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[[Category: Chi, Y I.]]
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[[Category: Crofts AR]]
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[[Category: Crofts, A R.]]
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[[Category: Huang L]]
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[[Category: Huang, L.]]
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[[Category: Hung LW]]
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[[Category: Hung, L W.]]
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[[Category: Kim KK]]
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[[Category: Kim, K K.]]
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[[Category: Kim SH]]
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[[Category: Kim, S H.]]
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[[Category: Shulmeister VM]]
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[[Category: Shulmeister, V M.]]
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[[Category: Zhang Z]]
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[[Category: Zhang, Z.]]
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[[Category: Membrane protein]]
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[[Category: Oxidoreductase]]
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[[Category: Redox enzyme]]
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[[Category: Respiratory chain]]
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[[Category: Stigmatellin]]
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[[Category: Ubiquinone]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:06:15 2008''
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Current revision

STIGMATELLIN-BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN

PDB ID 2bcc

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