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1occ

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[[Image:1occ.jpg|left|200px]]
[[Image:1occ.jpg|left|200px]]
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{{Structure
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|PDB= 1occ |SIZE=350|CAPTION= <scene name='initialview01'>1occ</scene>, resolution 2.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1occ", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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/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] </span>
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{{STRUCTURE_1occ| PDB=1occ | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1occ FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1occ OCA], [http://www.ebi.ac.uk/pdbsum/1occ PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1occ RCSB]</span>
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'''STRUCTURE OF BOVINE HEART CYTOCHROME C OXIDASE AT THE FULLY OXIDIZED STATE'''
'''STRUCTURE OF BOVINE HEART CYTOCHROME C OXIDASE AT THE FULLY OXIDIZED STATE'''
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[[Category: Yaono, R.]]
[[Category: Yaono, R.]]
[[Category: Yoshikawa, S.]]
[[Category: Yoshikawa, S.]]
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[[Category: cytochrome c oxidase]]
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[[Category: Cytochrome c oxidase]]
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[[Category: oxidoreductase (cytochrome(c)-oxygen)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:39:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:43:09 2008''
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Revision as of 00:39, 3 May 2008

Image:1occ.jpg

Template:STRUCTURE 1occ

STRUCTURE OF BOVINE HEART CYTOCHROME C OXIDASE AT THE FULLY OXIDIZED STATE


Overview

The crystal structure of bovine heart cytochrome c oxidase at 2.8 A resolution with an R value of 19.9 percent reveals 13 subunits, each different from the other, five phosphatidyl ethanolamines, three phosphatidyl glycerols and two cholates, two hemes A, and three copper, one magnesium, and one zinc. Of 3606 amino acid residues in the dimer, 3560 have been converged to a reasonable structure by refinement. A hydrogen-bonded system, including a propionate of a heme A (heme a), part of peptide backbone, and an imidazole ligand of CuA, could provide an electron transfer pathway between CuA and heme a. Two possible proton pathways for pumping, each spanning from the matrix to the cytosolic surfaces, were identified, including hydrogen bonds, internal cavities likely to contain water molecules, and structures that could form hydrogen bonds with small possible conformational change of amino acid side chains. Possible channels for chemical protons to produce H2O, for removing the produced water, and for O2, respectively, were identified.

About this Structure

1OCC is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

Reference

The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A., Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, Yaono R, Yoshikawa S, Science. 1996 May 24;272(5265):1136-44. PMID:8638158 Page seeded by OCA on Sat May 3 03:39:41 2008

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