3GQB

Crystal Structure of the A3B3 complex from V-ATPase

Summary for 3GQB

• Entry DOI: 10.2210/pdb3gqb/pdb
• Descriptor: V-type ATP synthase alpha chain, V-type ATP synthase beta chain (3 entities in total)
• Functional Keywords: a3b3, v-atpase, atp synthesis, atp-binding, hydrogen ion transport, hydrolase, ion transport, nucleotide-binding, transport
• Biological source: Thermus thermophilus HB8; More
• Total number of polymer chains: 4
• Total formula weight: 230520.88

Authors

Meher, M.,Akimoto, S.,Iwata, M.,Nagata, K.,Hori, Y.,Yoshida, M.,Yokoyama, S.,Iwata, S.,Yokoyama, K. (deposition date: 2009-03-24, release date: 2009-11-24, Last modification date: 2024-02-21)

Primary citation

Maher, M.J.,Akimoto, S.,Iwata, M.,Nagata, K.,Hori, Y.,Yoshida, M.,Yokoyama, S.,Iwata, S.,Yokoyama, K.
Crystal structure of A(3)B(3) complex of V-ATPase from Thermus thermophilus.
Embo J., 28:3771-3779, 2009

PubMed 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 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 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 F(o)F(1)-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.

PubMed: 19893485
DOI: 10.1038/emboj.2009.310

Experimental method

X-RAY DIFFRACTION (2.8 Å)