Priming a Molecular Motor for Disassembly Alastair G. Stewart, Daniela Stock  Structure  Volume 20, Issue 11, Pages 1799-1800 (November 2012) DOI: 10.1016/j.str.2012.10.003 Copyright © 2012 Elsevier Ltd Terms and Conditions

Figure 1 V-ATPase Assembly and Disassembly (A) Fully assembled complex with hydrolysis of ATP, rotation of central stalk, and direction of proton movement are indicated by arrows. (B) Bending of the EGC complex by RAVE (shown as a clockwork key) is required to assemble the intact V-ATPase. (C) Spring-load triggered disassembly of the V1 complex from Vo shuts down wasteful ATP hydrolysis. Structure 2012 20, 1799-1800DOI: (10.1016/j.str.2012.10.003) Copyright © 2012 Elsevier Ltd Terms and Conditions

Figure 2 Architectural Similarity of Peripheral Stalk Complexes and Their Propensity to Bend along Their Long Axes (A) F-ATPase peripheral stalk (Dickson et al., 2006). (B) A-ATPase peripheral stalk (Stewart et al., 2012). (C) Eukaryotic V-type peripheral stalk (Oot et al., 2012). Structure 2012 20, 1799-1800DOI: (10.1016/j.str.2012.10.003) Copyright © 2012 Elsevier Ltd Terms and Conditions