1ocr

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(New page: 200px<br /><applet load="1ocr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ocr, resolution 2.35&Aring;" /> '''BOVINE HEART CYTOCHR...)
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'''BOVINE HEART CYTOCHROME C OXIDASE IN THE FULLY REDUCED STATE'''<br />
'''BOVINE HEART CYTOCHROME C OXIDASE IN THE FULLY REDUCED STATE'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1OCR 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 and HEA 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OCR OCA].
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1OCR 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 <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=HEA:'>HEA</scene> 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OCR OCA].
==Reference==
==Reference==
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[[Category: reduced]]
[[Category: reduced]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:55:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:16:09 2008''

Revision as of 12:16, 21 February 2008

Image:1ocr.gif

1ocr, resolution 2.35Å

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BOVINE HEART CYTOCHROME C OXIDASE IN THE FULLY REDUCED 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

1OCR is a Protein complex structure of sequences from Bos taurus with , , , and as ligands. Active as Cytochrome-c oxidase, with EC number 1.9.3.1 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

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