2bcc

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[[Image:2bcc.gif|left|200px]]
[[Image:2bcc.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2bcc |SIZE=350|CAPTION= <scene name='initialview01'>2bcc</scene>, resolution 3.50&Aring;
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The line below this paragraph, containing "STRUCTURE_2bcc", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=BHI:HIS+Axial+Ligands+Of+High+Potential+Heme+Of+Cytochrome+B'>BHI</scene>, <scene name='pdbsite=BLO:HIS+Axial+Ligands+Of+Low+Potential+Heme+Of+Cytochrome+B'>BLO</scene>, <scene name='pdbsite=C1H:HIS+And+MET+Axial+Ligands+Of+High+Potential+Heme+Of+Cyto+...'>C1H</scene> and <scene name='pdbsite=FES:HIS+And+Cystine+Ligands+Of+Rieske+Fe-S+Cluster'>FES</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <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:PHOSPHATIDYLETHANOLAMINE'>PEE</scene>, <scene name='pdbligand=SIG:STIGMATELLIN'>SIG</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</scene>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_2bcc| PDB=2bcc | SCENE= }}
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|RELATEDENTRY=[[1bcc|1BCC]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bcc OCA], [http://www.ebi.ac.uk/pdbsum/2bcc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bcc RCSB]</span>
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}}
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'''STIGMATELLIN-BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN'''
'''STIGMATELLIN-BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN'''
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[[Category: Shulmeister, V M.]]
[[Category: Shulmeister, V M.]]
[[Category: Zhang, Z.]]
[[Category: Zhang, Z.]]
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[[Category: membrane protein]]
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[[Category: Membrane protein]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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[[Category: redox enzyme]]
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[[Category: Redox enzyme]]
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[[Category: respiratory chain]]
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[[Category: Respiratory chain]]
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[[Category: stigmatellin]]
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[[Category: Stigmatellin]]
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[[Category: ubiquinone]]
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:04:16 2008''
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Revision as of 17:06, 3 May 2008

Image:2bcc.gif

Template:STRUCTURE 2bcc

STIGMATELLIN-BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN


Overview

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.

About this Structure

2BCC is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 20:06:15 2008

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