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

The EMBO Journal | WILEY | Published : 2009

Abstract

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..

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University of Melbourne Researchers

Grants

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


Awarded by Targeted Proteins Research Program (TPRP)


Awarded by Grants-in-Aid for Scientific Research


Awarded by Biotechnology and Biological Sciences Research Council


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.