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Logo of jbcThe Journal of Biological Chemistry
J Biol Chem. 2015 February 6; 290(6): 3197.
PMCID: PMC4318994

Exploring the Fine Structural Details of Eukaryotic V1VO-ATPases and Their Activity♦

Crystal Structure of Subunits D and F in Complex Give Insight into Energy Transmission of the Eukaryotic V-ATPase from Saccharomyces cerevisiae

♦ See referenced article, J. Biol. Chem. 2015, 290, 3183–3196

Eukaryotic V1VO-ATPases hydrolyze ATP to generate an electrochemical proton gradient across membranes. The activity of V-ATPases is regulated by the reversible disassembly of the V1 and VO domains. Two subunits, called D and F, are thought to be critical in overseeing the reversible disassembly and the ATPase activity and ion conduction of the V-ATPase. D and F come together to form the DF subunit that is the main motor for the ATPase. In this Paper of the Week, a team led by Gerhard Grüber at the Nanyang Technological University in Singapore analyzed two conformations of the DF subunit of Saccharomyces cerevisiae (ScDF) V-ATPase at 3.1 Å resolution. The investigators found that structural elements in the individual D and F subunits, such as helices at the ends of the domains and flexible loops, allowed the DF subunit to assemble and do its job as the enzyme's motor. The authors say, “The new structures shed light onto the coupling events of ATP-dependent ion pumping and reversible disassembly.”

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Fitting of the ScDF onto the DF subunits of the nucleotide-bound Enterococcus hirae A1-ATP synthase structure.

Articles from The Journal of Biological Chemistry are provided here courtesy of American Society for Biochemistry and Molecular Biology