Missing pieces Image credit – Daniel Schep
Vacuolar-type ATPases (V-ATPases) are ATP-powered proton pumps involved in numerous essential processes in the cell. The Rubinstein laboratory has recently used cryo-EM to determine 3D structures of the V-ATPase (Zhao et al. 2015, Nature) and the related mitochondrial ATP synthase (Zhou et al. 2015, eLife). These cryo-EM studies have also demonstrated remarkable conformational heterogeneity in the enzymes. While conformational heterogeneity is biologically interesting, it has limited the ability to get atomic resolution structures of ATPases, particularly for one of the key membrane-embedded subunits. In this manuscript Schep et al. combine cryo-EM studies with the use of information from evolutionary covariance to build a first atomic model for the membrane-embedded subunits from a bacterial V/A-ATPase and the eukaryotic V-ATPase. The models show a surprising conservation of architecture in all rotary ATPases.
This paper is published in the Proceedings of the National Academy of Science (PNAS): http://www.ncbi.nlm.nih.gov/pubmed/26951669
