1occ
From Proteopedia
(New page: 200px<br /><applet load="1occ" size="450" color="white" frame="true" align="right" spinBox="true" caption="1occ, resolution 2.8Å" /> '''STRUCTURE OF BOVINE H...) |
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| - | [[Image:1occ.jpg|left|200px]]<br /><applet load="1occ" size=" | + | [[Image:1occ.jpg|left|200px]]<br /><applet load="1occ" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1occ, resolution 2.8Å" /> | caption="1occ, resolution 2.8Å" /> | ||
'''STRUCTURE OF BOVINE HEART CYTOCHROME C OXIDASE AT THE FULLY OXIDIZED STATE'''<br /> | '''STRUCTURE OF BOVINE HEART CYTOCHROME C OXIDASE AT THE FULLY OXIDIZED STATE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of bovine heart cytochrome c oxidase at 2.8 A | + | 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== | ==About this Structure== | ||
| - | 1OCC 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, 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:// | + | 1OCC 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=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=1OCC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: oxidoreductase (cytochrome(c)-oxygen)]] | [[Category: oxidoreductase (cytochrome(c)-oxygen)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:16:02 2008'' |
Revision as of 12:16, 21 February 2008
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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 with , , and as ligands. Active as Cytochrome-c oxidase, with EC number 1.9.3.1 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
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