1bcc
From Proteopedia
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|PDB= 1bcc |SIZE=350|CAPTION= <scene name='initialview01'>1bcc</scene>, resolution 3.16Å | |PDB= 1bcc |SIZE=350|CAPTION= <scene name='initialview01'>1bcc</scene>, resolution 3.16Å | ||
|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> | |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> | ||
| - | |LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand= | + | |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=U10:UBIQUINONE-10'>U10</scene>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene> |
| - | |ACTIVITY= [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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bcc OCA], [http://www.ebi.ac.uk/pdbsum/1bcc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bcc RCSB]</span> | ||
}} | }} | ||
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[[Category: Shulmeister, V M.]] | [[Category: Shulmeister, V M.]] | ||
[[Category: Zhang, Z.]] | [[Category: Zhang, Z.]] | ||
| - | [[Category: BOG]] | ||
| - | [[Category: FES]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: PEE]] | ||
| - | [[Category: U10]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
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[[Category: ubiquinone]] | [[Category: ubiquinone]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:58:00 2008'' |
Revision as of 15:58, 30 March 2008
| |||||||
| , resolution 3.16Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Ligands: | , , , , , | ||||||
| Activity: | Ubiquinol--cytochrome-c reductase, with EC number 1.10.2.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
1BCC is a Protein complex structure of sequences 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 Sun Mar 30 18:58:00 2008
Categories: Gallus gallus | Protein complex | Ubiquinol--cytochrome-c reductase | Berry, E A. | Chi, Y I. | Crofts, A R. | Huang, L. | Hung, L W. | Kim, K K. | Kim, S H. | Shulmeister, V M. | Zhang, Z. | Electron transport | Membrane protein | Oxidoreductase | Redox enzyme | Respiratory chain | Ubiquinone
