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@article{1762522, author = {Pinke, G. and Zhou, L. and Sazanov, L.A.}, article_location = {NEW YORK}, article_number = {11}, doi = {http://dx.doi.org/10.1038/s41594-020-0503-8}, keywords = {MITOCHONDRIAL PERMEABILITY TRANSITION; C-SUBUNIT; COMPLEX I; ATOMIC MODEL; ARCHITECTURE; PREDICTION; CHANNEL; REGION; DIMERS; MOTION}, language = {eng}, issn = {1545-9993}, journal = {NATURE STRUCTURAL & MOLECULAR BIOLOGY}, title = {Cryo-EM structure of the entire mammalian F-type ATP synthase}, url = {https://www.nature.com/articles/s41594-020-0503-8}, volume = {27}, year = {2020} }
TY - JOUR ID - 1762522 AU - Pinke, G. - Zhou, L. - Sazanov, L.A. PY - 2020 TI - Cryo-EM structure of the entire mammalian F-type ATP synthase JF - NATURE STRUCTURAL & MOLECULAR BIOLOGY VL - 27 IS - 11 SP - 1077 EP - 1077 PB - NATURE PUBLISHING GROUP SN - 15459993 KW - MITOCHONDRIAL PERMEABILITY TRANSITION KW - C-SUBUNIT KW - COMPLEX I KW - ATOMIC MODEL KW - ARCHITECTURE KW - PREDICTION KW - CHANNEL KW - REGION KW - DIMERS KW - MOTION UR - https://www.nature.com/articles/s41594-020-0503-8 N2 - The majority of adenosine triphosphate (ATP) powering cellular processes in eukaryotes is produced by the mitochondrial F1Fo ATP synthase. Here, we present the atomic models of the membrane Fo domain and the entire mammalian (ovine) F1Fo, determined by cryo-electron microscopy. Subunits in the membrane domain are arranged in the 'proton translocation cluster' attached to the c-ring and a more distant 'hook apparatus' holding subunit e. Unexpectedly, this subunit is anchored to a lipid 'plug' capping the c-ring. We present a detailed proton translocation pathway in mammalian Fo and key inter-monomer contacts in F1Fo multimers. Cryo-EM maps of F1Fo exposed to calcium reveal a retracted subunit e and a disassembled c-ring, suggesting permeability transition pore opening. We propose a model for the permeability transition pore opening, whereby subunit e pulls the lipid plug out of the c-ring. Our structure will allow the design of drugs for many emerging applications in medicine. Cryo-EM structures of the entire mammalian F1Fo ATPase reveal several new features and details on the proton translocation pathway and suggest a model for the opening of the permeability transition pore. ER -
PINKE, G., L. ZHOU and L.A. SAZANOV. Cryo-EM structure of the entire mammalian F-type ATP synthase. \textit{NATURE STRUCTURAL \&{}amp; MOLECULAR BIOLOGY}. NEW YORK: NATURE PUBLISHING GROUP, 2020, vol.~27, No~11, p.~1077-1101. ISSN~1545-9993. Available from: https://dx.doi.org/10.1038/s41594-020-0503-8.
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