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

DOI: 10.1038/emboj.2009.310 DOI Help

Authors: Megan Maher (Imperial College Londo) , Satoru Akimoto (RIKEN) , Momi Iwata (Diamond Light Source) , Koji Nagata (Imperial College London) , Yoshiko Hori (RIKEN) , Masasuke Yoshida (Tokyo Inst Technol) , Shigeyuki Yokoyama (RIKEN) , Ken Yokoyama (RIKEN) , So Iwata (Diamond Light Source)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: The Embo Journal , VOL 28 (23) , PAGES 3771-3779

State: Published (Approved)
Published: November 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 A3B3 subcomplex of V?ATPase at 2.8 Å resolution. The overall construction of the A3B3 subcomplex is significantly different from that of the ?3?3 sub?domain in FoF1?ATP synthase, because of the presence of a protruding ‘bulge’ domain feature in the catalytic A subunits. The A3B3 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 A3B3 structure, has highlighted the presence of a cluster composed of key hydrophobic residues, which are essential for ATP hydrolysis by V?ATPases.

Journal Keywords: Crystal Structure; Fof1; Proton Pump; Rotary Motor; V-Atpase

Subject Areas: Biology and Bio-materials

Diamond Offline Facilities: Membrane Protein Laboratory (MPL)

Facility: ESRF