
Cytochrome oxidase: structural insights from electron microscopy and from secondary structure prediction.
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.
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Related Subject Headings
- Protein Conformation
- Microscopy, Electron
- Membrane Proteins
- Macromolecular Substances
- Lipid Bilayers
- Inorganic & Nuclear Chemistry
- Immunologic Techniques
- Immunoglobulin Fab Fragments
- Freeze Fracturing
- Freeze Drying
Citation

Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Protein Conformation
- Microscopy, Electron
- Membrane Proteins
- Macromolecular Substances
- Lipid Bilayers
- Inorganic & Nuclear Chemistry
- Immunologic Techniques
- Immunoglobulin Fab Fragments
- Freeze Fracturing
- Freeze Drying