Journal article
Crystal structure of A3B3 complex of V-ATPase from Thermus thermophilus
MJ Maher, S Akimoto, M Iwata, K Nagata, Y Hori, M Yoshida, S Yokoyama, S Iwata, K Yokoyama
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 resolution. The overall construction of the A 3 B 3 subcomplex is significantly different from that of the α 3 Β 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. Specifically, ..
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Awarded by Japan Society for the Promotion of Science
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.