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ABSTRACT:
SUBMITTER: Maher MJ
PROVIDER: S-EPMC2775895 | biostudies-literature | 2009 Dec
REPOSITORIES: biostudies-literature
Maher Megan J MJ Akimoto Satoru S Iwata Momi M Nagata Koji K Hori Yoshiko Y Yoshida Masasuke M Yokoyama Shigeyuki S Iwata So S Yokoyama Ken K
The EMBO journal 20091105 23
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 ...[more]