Crystal structure of A3B3 complex of V-ATPase from Thermus thermophilus

被引:48
作者
Maher, Megan J. [1 ]
Akimoto, Satoru [2 ]
Iwata, Momi [1 ,3 ]
Nagata, Koji [1 ]
Hori, Yoshiko [2 ]
Yoshida, Masasuke [4 ,5 ]
Yokoyama, Shigeyuki [2 ]
Iwata, So [1 ,3 ,6 ,7 ]
Yokoyama, Ken [2 ,4 ,5 ]
机构
[1] Univ London Imperial Coll Sci Technol & Med, Div Mol Biosci, London SW7 2AZ, England
[2] RIKEN, Yokohama Inst, Prot Res Grp, Genom Sci Ctr,Tsurumi Ki, Yokohama, Kanagawa, Japan
[3] Diamond Light Source Ltd, Membrane Prot Lab, Didcot, Oxon, England
[4] Tokyo Inst Technol, Chem Resources Lab, Midori Ku, Yokohama, Kanagawa 227, Japan
[5] Natl Museum Emerging Sci & Innovat, Japan Sci & Technol Agcy, ATP Synth Regulat Project, ICORP,Koto Ku, Tokyo, Japan
[6] Kyoto Univ, Fac Med, Dept Cell Biol, Sakyo Ku, Kyoto, Japan
[7] Japan Sci & Technol Agcy, Human Receptor Crystallog Project, Exploratory Res Adv Technol ERATO, Sakyo Ku, Kyoto, Japan
关键词
crystal structure; FoF1; proton pump; rotary motor; V-ATPase; CATALYTIC SITES; MUTATIONAL ANALYSIS; SUBUNIT-A; BINDING; SYNTHASE; HYDROLYSIS; MECHANISM; ROTATION; F1-ATPASE;
D O I
10.1038/emboj.2009.310
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 angstrom 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 FoF1-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, in the non-catalytic interface, the B subunit seems to be incapable of binding ATP, which is a marked difference from the situation indicated by the structure of the FoF1-ATP synthase. In the catalytic interface, our mutational analysis, on the basis of the A(3)B(3) structure, has highlighted the presence of a cluster composed of key hydrophobic residues, which are essential for ATP hydrolysis by V-ATPases. The EMBO Journal (2009) 28, 3771-3779. doi: 10.1038/emboj.2009.310; Published online 5 November 2009
引用
收藏
页码:3771 / 3779
页数:9
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