Journal article

Crystal structure of A(3)B(3) complex of V-ATPase from Thermus thermophilus

Megan J Maher, Satoru Akimoto, Momi Iwata, Koji Nagata, Yoshiko Hori, Masasuke Yoshida, Shigeyuki Yokoyama, So Iwata, Ken Yokoyama

EMBO JOURNAL | WILEY | Published : 2009


Vacuolar-type ATPases (V-ATPases) exist in various cellular membranes of many organisms to regulate physiological processes by controlling the acidic environment. Here, we have determined the crystal structure of the A(3)B(3) subcomplex of V-ATPase at 2.8 A resolution. The overall construction of the A(3)B(3) subcomplex is significantly different from that of the alpha(3)beta(3) sub-domain in F(o)F(1)-ATP synthase, because of the presence of a protruding 'bulge' domain feature in the catalytic A subunits. The A(3)B(3) subcomplex structure provides the first molecular insight at the catalytic and non-catalytic interfaces, which was not possible in the structures of the separate subunits alone..

View full abstract

University of Melbourne Researchers


Awarded by Ministry of Education, Science, Sports and Culture of Japan

Awarded by Targeted Proteins Research Program (TPRP)

Awarded by Biotechnology and Biological Sciences Research Council

Awarded by Grants-in-Aid for Scientific Research

Funding Acknowledgements

We thank S Hayashi, T Ikegami and Y Suzuki for critical discussion, members of Hisabori and Yoshida laboratories, Diamond MPL and ICORP in Odaiba for help and advice, T Yano for laboratory management and encouragement. This work was partly supported by Grants-in-Aid from the Ministry of Education, Science, Sports and Culture of Japan to KY (No. 21023009 and 21370042), Targeted Proteins Research Program (TPRP) (B-37, to KY), Welcome Trust to MI, and a Cancer Institute of NSW fellowship (MJM). We thank a referee who suggested the possible twinning problem of the structure.