1oco
From Proteopedia
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| - | [[Image:1oco.gif|left|200px]] | + | [[Image:1oco.gif|left|200px]] |
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| - | '''BOVINE HEART CYTOCHROME C OXIDASE IN CARBON MONOXIDE-BOUND STATE''' | + | {{Structure |
| + | |PDB= 1oco |SIZE=350|CAPTION= <scene name='initialview01'>1oco</scene>, resolution 2.8Å | ||
| + | |SITE= <scene name='pdbsite=CXB:C+Monoxide+Binding+Site'>CXB</scene> | ||
| + | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene> and <scene name='pdbligand=CMO:CARBON MONOXIDE'>CMO</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Cytochrome-c_oxidase Cytochrome-c oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''BOVINE HEART CYTOCHROME C OXIDASE IN CARBON MONOXIDE-BOUND STATE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OCO is a [ | + | 1OCO is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. The following pages contain interesting information on the relation of 1OCO with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb5_1.html Cytochrome c Oxidase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OCO OCA]. |
==Reference== | ==Reference== | ||
| - | Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase., Yoshikawa S, Shinzawa-Itoh K, Nakashima R, Yaono R, Yamashita E, Inoue N, Yao M, Fei MJ, Libeu CP, Mizushima T, Yamaguchi H, Tomizaki T, Tsukihara T, Science. 1998 Jun 12;280(5370):1723-9. PMID:[http:// | + | Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase., Yoshikawa S, Shinzawa-Itoh K, Nakashima R, Yaono R, Yamashita E, Inoue N, Yao M, Fei MJ, Libeu CP, Mizushima T, Yamaguchi H, Tomizaki T, Tsukihara T, Science. 1998 Jun 12;280(5370):1723-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9624044 9624044] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Cytochrome c]] | [[Category: Cytochrome c]] | ||
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[[Category: oxidoreductase (cytochrome(c)-oxygen)]] | [[Category: oxidoreductase (cytochrome(c)-oxygen)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:09:02 2008'' |
Revision as of 11:09, 20 March 2008
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| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , , and | ||||||
| Activity: | Cytochrome-c oxidase, with EC number 1.9.3.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BOVINE HEART CYTOCHROME C OXIDASE IN CARBON MONOXIDE-BOUND STATE
Overview
Crystal structures of bovine heart cytochrome c oxidase in the fully oxidized, fully reduced, azide-bound, and carbon monoxide-bound states were determined at 2.30, 2.35, 2.9, and 2.8 angstrom resolution, respectively. An aspartate residue apart from the O2 reduction site exchanges its effective accessibility to the matrix aqueous phase for one to the cytosolic phase concomitantly with a significant decrease in the pK of its carboxyl group, on reduction of the metal sites. The movement indicates the aspartate as the proton pumping site. A tyrosine acidified by a covalently linked imidazole nitrogen is a possible proton donor for the O2 reduction by the enzyme.
About this Structure
1OCO is a Protein complex structure of sequences from Bos taurus. The following pages contain interesting information on the relation of 1OCO with [Cytochrome c Oxidase]. Full crystallographic information is available from OCA.
Reference
Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase., Yoshikawa S, Shinzawa-Itoh K, Nakashima R, Yaono R, Yamashita E, Inoue N, Yao M, Fei MJ, Libeu CP, Mizushima T, Yamaguchi H, Tomizaki T, Tsukihara T, Science. 1998 Jun 12;280(5370):1723-9. PMID:9624044
Page seeded by OCA on Thu Mar 20 13:09:02 2008
