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

• Megan J Maher ^[1] ; Satoru Akimoto ^[3] ; Momi Iwata ^[1] ; Koji Nagata ^[1] ; Yoshiko Hori ^[3] ; Masasuke Yoshida ^[2] ; Shigeyuki Yokoyama ^[3] ; So Iwata ; Ken Yokoyama ^[4]
  1. [1] Imperial College London

     Imperial College London

     Reino Unido

     
  2. [2] Tokyo Institute of Technology

     Tokyo Institute of Technology

     Japón

     
  3. [3] Protein Research Group, Genomic Sciences Center, Yokohama Institute, RIKEN, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Japan
  4. [4] Protein Research Group, Genomic Sciences Center, Yokohama Institute, RIKEN, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Japan; Chemical Resources Laboratory, Tokyo Institute of Technology, Midori-ku, Yokohama, Japan; ICORP, ATP Synthesis Regulation Project, Japan Science and Technology Agency, National Museum of Emerging Science and Innovation, Koto-ku, Tokyo, Japan

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• Localización: EMBO journal: European Molecular Biology Organization, ISSN 0261-4189, Vol. 28, Nº. 23, 2009, págs. 3771-3779
• Idioma: inglés
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• Resumen

  • 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 α3β3 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.