A model for the structure of the yeast mitochondrial adenosine triphosphatase complex.
Monodisperse, Triton-solubilized ATPase complex was treated with the reversible protein-protein cross-linker dithiobis(succinimidyl)propionate under conditions where only intracomplex cross-links were formed. The resulting products were analyzed by two-dimensional sodium dodecyl sulfate-acrylamide slab gel electrophoresis under reducing and oxidizing conditions. Using the observed major subunit-subunit cross-links and the previously published subunit stoichiometries (Todd, R., Griesenbeck, T., and Douglas, M. (1980) J. Biol. Chem. 255, 5461-5467), a model of the ATPase complex was constructed. The model is a closed structure which could be formed by self-limited assembly of the subunits. The model also has the novel features of a pseudo-mirror symmetry and clustering of mitochondrially and nuclearly coded subunits into two different domains.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D003432:Cross-Linking Reagents; D004220:Disulfides; D046911:Macromolecular Substances; D008928:Mitochondria / Q000201:enzymology*; D008970:Molecular Weight; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013388:Succinimides
D003432:Cross-Linking Reagents; D004220:Disulfides; D046911:Macromolecular Substances; D013388:Succinimides; D000251:Adenosine Triphosphatases; C011240:dithiobis(succinimidylpropionate)