1occ

From Proteopedia

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 CU, MG, ZN and HEA 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

Page seeded by OCA on Tue Nov 20 22:54:33 2007