title: Priming a molecular motor for disassembly.
abstract: In this issue of Structure, Oot and colleagues present the crystal structure of the eukaryotic V-ATPase peripheral stalk in complex with one of its binding partners, revealing conformational flexibility that may be important for priming the complex for rapid disassembly in response to external stimuli.
authors.affiliation: The Victor Chang Cardiac Research Institute, Sydney NSW 2010, Australia. a.stewart@victorchang.edu.au
authors.forename: Alastair G
authors.initials: AG
authors.lastname: Stewart
authors.forename: Daniela
authors.initials: D
authors.lastname: Stock
mesh_terms: D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D025262:Vacuolar Proton-Translocating ATPases / Q000378:metabolism*
chemical_list: D025262:Vacuolar Proton-Translocating ATPases