2occ
From Proteopedia
(New page: 200px<br /> <applet load="2occ" size="450" color="white" frame="true" align="right" spinBox="true" caption="2occ, resolution 2.3Å" /> '''BOVINE HEART CYTOCHR...) |
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==About this Structure== | ==About this Structure== | ||
| - | 2OCC is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]] with CU, MG, NA, ZN, HEA and PER as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2OCC OCA]]. | + | 2OCC is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]] with CU, MG, NA, ZN, HEA and PER as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Site: PXB. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2OCC 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9624044 9624044] | 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9624044 9624044] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
| + | [[Category: Cytochrome-c oxidase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Tsukihara, T.]] | [[Category: Tsukihara, T.]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:33:04 2007'' |
Revision as of 12:28, 30 October 2007
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BOVINE HEART CYTOCHROME C OXIDASE AT THE FULLY OXIDIZED 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
2OCC is a [Protein complex] structure of sequences from [Bos taurus] with CU, MG, NA, ZN, HEA and PER as [ligands]. Active as [Cytochrome-c oxidase], with EC number [1.9.3.1]. Structure known Active Site: PXB. 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 Tue Oct 30 14:33:04 2007
Categories: Bos taurus | Cytochrome-c oxidase | Protein complex | Tsukihara, T. | Yao, M. | CU | HEA | MG | NA | PER | ZN | Cytochrome c oxidase | Cytochrome(c)-oxygen | Oxidoreductase
