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Electron cryomicroscopy of rotary ATPases
Author(s) -
Rubinstein John L.
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.259.4
Subject(s) - atp hydrolysis , atp synthase , cryo electron microscopy , atpase , molecular motor , adenosine triphosphate , biophysics , transmembrane protein , molecular machine , v atpase , transmembrane domain , chemiosmosis , chemistry , biochemistry , enzyme , biology , nanotechnology , membrane , materials science , receptor
Ion‐translocating rotary ATPases serve either as adenosine triphosphate (ATP) synthases, using energy from a transmembrane ion motive force to create the cell's supply of ATP, or as transmembrane ion pumps that are powered by ATP hydrolysis. The members of this family of enzymes each contain two rotary motors: one that couples ion translocation to rotation and one that couples rotation to ATP synthesis or hydrolysis. Our group uses electron cryomicroscopy (cryo‐EM) of single protein particles to study the structures of rotary ATPases. We also work to develop new methods for cryo‐EM to facilitate these studies. Our recent studies have not only illuminated the structures of these fascinating molecular motors at unprecedented resolution, but have also started to uncover their dynamics through computational isolation of the different conformations of the enzymes that exist simultaneously in solution. This lecture will describe the latest structures we have determined for the mitochondrial ATP synthase and proton pumping V‐ATPase, and what we have learned about how these enzymes function and how they interact with molecules that affect their activities. Support or Funding Information Canadian Institutes of Health Research, Canada Research Chairs