vacuolar type ATPase (V-ATPase) is a highly conserved ancient enzyme with remarkably diverse functions in various eukaryotes and some bacteria. Like F ATPase, it consists of 2 domains V1 and Vo and has rotary mechanism coupling ATP synthesis and hydrolysis. The C subunit of this enzyme has a cavity and acts as socket to attach two domains. This is essential for association and dissociation of two domains for regulation of ATPase activity. The target of this jmol is to study different aspects of this subunit in comparison to other prokaryotes and eukaryotes.
| Structure of C subunit of V ATPase from T. thermophilus | Page 1 |
| Structure of C subunit of V ATPase | Page 2 |
| Subunit C of V ATPase with 3 different views | Page 3 |
| Comparision of subunit C of 2 different bacteria | Page 4 |
| F ATPase from eukaryotes (yeast) | Page 5 |
| Crystal structure of the nucleotide-free alpha beta subcomplex of F1-ATPase from the thermophilic Bacillus PS3 | Page 6 |
| Comparision between subunit C of bacteria and yeast | Page 7 |