1OCC
STRUCTURE OF BOVINE HEART CYTOCHROME C OXIDASE AT THE FULLY OXIDIZED STATE
Summary for 1OCC
Entry DOI | 10.2210/pdb1occ/pdb |
Descriptor | CYTOCHROME C OXIDASE, COPPER (II) ION, MAGNESIUM ION, ... (17 entities in total) |
Functional Keywords | cytochrome c oxidase, oxidoreductase (cytochrome(c)-oxygen) |
Biological source | Bos taurus (cattle) More |
Cellular location | Mitochondrion inner membrane; Multi-pass membrane protein: P00396 P68530 P00415 Mitochondrion inner membrane: P07470 P13183 P00430 P10175 P00423 P00426 P00428 P07471 P04038 Mitochondrion intermembrane space: P00429 |
Total number of polymer chains | 26 |
Total formula weight | 413609.27 |
Authors | Tsukihara, T.,Aoyama, H.,Yamashita, E.,Tomizaki, T.,Yamaguchi, H.,Shinzawa-Itoh, K.,Nakashima, R.,Yaono, R.,Yoshikawa, S. (deposition date: 1996-04-18, release date: 1996-12-07, Last modification date: 2018-03-21) |
Primary citation | Tsukihara, T.,Aoyama, H.,Yamashita, E.,Tomizaki, T.,Yamaguchi, H.,Shinzawa-Itoh, K.,Nakashima, R.,Yaono, R.,Yoshikawa, S. The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A. Science, 272:1136-1144, 1996 Cited by PubMed Abstract: 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. PubMed: 8638158PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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