Ion-translocating rotary ATPases serve either as 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.  These remarkable molecular machines are large and unstable membrane protein complexes and consequently their structures can not easily be determined by traditional methods.  Our group uses and develops the tools of single particle electron cryomicroscopy (cryo-EM) to study these macromolecular assemblies.  In cryo-EM, purified protein complexes are embedded in a film of amorphous ice by rapid freezing, and 3-D structures of the protein complex are calculated from transmission electron microscope images of the protein.  Recent results from cryo-EM of a variety of rotary ATPases will be presented.

Electron cryomicroscopy of rotary ATPases

245th National Meeting (2013)

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