Nucleotide-free V1EG domain of V/A-ATPase from Thermus thermophilus, state2

Structural snapshots of V/A-ATPase reveal the rotary catalytic mechanism of rotary ATPases.

The atomic model built in this study was used as an initial model.

Japan Society for the Promotion of Science (JSPS)

Japan Agency for Medical Research and Development (AMED)

Ministry of Education, Culture, Sports, Science and Technology (Japan)

For V-ATPase subunit A, the bacterium has two mutations in its genome (S232A and T235S).

rotary ATPase, V-type ATPase, ATP synthase, Thermus thermophilus, chemo-mechanical coupling, MOTOR PROTEIN