title: The study of vacuolar-type ATPases by single particle electron microscopy.
abstract: Nature's molecular machines often work through the concerted action of many different protein subunits, which can give rise to large structures with complex activities. Vacuolar-type ATPases (V-ATPases) are membrane-embedded protein assemblies with a unique rotary catalytic mechanism. The dynamic nature and instability of V-ATPases make structural and functional studies of these enzymes challenging. Electron microscopy (EM) techniques, especially single particle electron cryomicroscopy (cryo-EM) and negative-stain EM, have provided extensive insight into the structure and function of these protein complexes. This minireview outlines what has been learned about V-ATPases using electron microscopy, highlights current challenges for their structural study, and discusses what cryo-EM will allow us to learn about these fascinating enzymes in the future.
authors.affiliation: a The Hospital for Sick Children Research Institute, 686 Bay Street, Toronto, ON M5G 0A4, Canada.
authors.forename: Jianhua
authors.initials: J
authors.lastname: Zhao
authors.forename: John L
authors.initials: JL
authors.lastname: Rubinstein
mesh_terms: D000818:Animals; D020285:Cryoelectron Microscopy / Q000379:methods*; D006801:Humans; D025262:Vacuolar Proton-Translocating ATPases / Q000648:ultrastructure*
chemical_list: D025262:Vacuolar Proton-Translocating ATPases
keywords: ATPase de type vacuolaire; V-ATPase; cryo-EM; cryo-ME; cryomicroscopie électronique; electron cryomicroscopy; electron microscopy; microscopie électronique; vacuolar-type ATPase