Cytochrome oxidase: structural insights from electron microscopy and from secondary structure prediction.

Journal Article (Journal Article)

Electron microscopic images of selectively contrasted cytochrome oxidase dimer crystals are interpreted in a manner consistent with the structure of monomers determined by Fuller et al. (J. Molec. Biol. 134, 305-327). The arms of the y-shaped monomers lie within and perpendicular to the lipid bilayer protruding approximately 25 A on the matrix side of the membrane. The cytoplasmic-side tails of two monomers spread apart in a dimer forming a large cleft. Decoration of the exposed matrix side of vesicle crystals with antisubunit IV antibody fragments indicates that subunit IV lies along the a-crystal axis roughly 20 A from the center of the dimer. A membrane propensity algorithm applied to the sequences of cytochrome oxidase subunits predicts a total of 19 transmembrane alpha-helices per monomer.

Full Text

Duke Authors

Cited Authors

  • Frey, TG; Kuhn, LA; Leigh, JS; Costello, MJ; Chan, SH

Published Date

  • March 1, 1985

Published In

Volume / Issue

  • 23 / 3-4

Start / End Page

  • 155 - 162

PubMed ID

  • 2991452

International Standard Serial Number (ISSN)

  • 0162-0134

Digital Object Identifier (DOI)

  • 10.1016/0162-0134(85)85020-0


  • eng

Conference Location

  • United States