Abstract
•Recent findings of cryo-EM structures of mammalian F1FO-ATPase.•The membrane-embedded domain of the F1FO-ATPase and the permeability transition pore.•The Ca2+-activated 1FO-ATPase role in the mPTP is consistent with recent cryo-EM findings.•The membrane-embedded FO participates in mPTP formation in mammalian mitochondria.•Conformational changes within FO modify the inner mitochondrial membrane shape.
Highlights
The cryo-EM structures of the entire mammalian complex allowed to identify the different substeps of the rotational state and improved knowledge on some up to now misinterpreted subunits of the membrane domain FO [2,3]
The F-type (F1FO) ATPase is composed of a hydrophilic catalytic F1 domain protruding in the mitochondrial matrix, where ATP synthesis/hydrolysis takes place, and a membrane-embedded FO domain that drives H+ translocation (Fig. 1A)
During the catalytic cycle of ATP hydrolysis the rotational states of mammalian mitochondrial F1-ATPase observed within a single 120° rotation shows 90° and 30° substeps, which differ from bacterial ones (80° and 40°, respectively) [7]
Summary
The cryo-EM structures of the entire mammalian complex allowed to identify the different substeps of the rotational state and improved knowledge on some up to now misinterpreted subunits of the membrane domain FO [2,3]. The F-type (F1FO) ATPase is composed of a hydrophilic catalytic F1 domain protruding in the mitochondrial matrix, where ATP synthesis/hydrolysis takes place, and a membrane-embedded FO domain that drives H+ translocation (Fig. 1A).
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