Abstract
Membrane-anchored AAA proteases are conserved ATP-dependent molecular machines that mediate the processing and turnover of membrane embedded proteins. We have determined the 12-Å resolution single-particle cryoEM structure of a full-length, hetero-oligomeric, yeast m-AAA protease hexamer, which reveals for the first time the structural organization of the membrane spanning and intermembrane space domains. The fitted structure of the intact protease offers an explanation how m-AAA proteases dislocate and degrade membrane integral proteins, and provides the stereo-chemical framework for further biochemical and mechanistic studies. The structure and mechanism of the m-AAA protease will be discussed.
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