Crystal structure of A3B3 complex of V-ATPase from Thermus thermophilus
Open Access
- 5 November 2009
- journal article
- research article
- Published by Springer Science and Business Media LLC in The EMBO Journal
- Vol. 28 (23), 3771-3779
- https://doi.org/10.1038/emboj.2009.310
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 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.Keywords
This publication has 44 references indexed in Scilit:
- Roles of Tyr122-hydrophobic Cluster and K+ Binding in Ca2+-releasing Process of ADP-insensitive Phosphoenzyme of Sarcoplasmic Reticulum Ca2+-ATPasePublished by Elsevier BV ,2008
- ATP Hydrolysis and Synthesis of a Rotary Motor V-ATPase from Thermus thermophilusPublished by Elsevier BV ,2008
- Phasercrystallographic softwareJournal of Applied Crystallography, 2007
- Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPaseThe EMBO Journal, 2006
- Crystal Structure of the Archaeal A1AO ATP Synthase Subunit B from Methanosarcina mazei Gö1: Implications of Nucleotide-binding Differences in the Major A1AO Subunits A and BJournal of Molecular Biology, 2006
- Coot: model-building tools for molecular graphicsActa Crystallographica Section D-Biological Crystallography, 2004
- Refinement of Macromolecular Structures by the Maximum-Likelihood MethodActa Crystallographica Section D-Biological Crystallography, 1997
- [20] Processing of X-ray diffraction data collected in oscillation modeMethods in Enzymology, 1997
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994