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Title: Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states
Authors: Sobti, Meghna
Smits, Callum
Ishmukhametov, Robert
Stock, Daniela
Sandin, Sara
Stewart, Alastair G
Wong, Andrew See Weng
Keywords: Cryo-EM
E. Coli ATP Synthase
DRNTU::Science::Biological sciences
Issue Date: 2016
Source: Sobti, M., Smits, C., Wong, A. S. W., Ishmukhametov, R., Stock, D., Sandin, S., & Stewart, A. G. (2016). Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states. eLife, 5, e21598-. doi:10.7554/eLife.21598
Series/Report no.: eLife
Abstract: A molecular model that provides a framework for interpreting the wealth of functional information obtained on the E. coli F-ATP synthase has been generated using cryo-electron microscopy. Three different states that relate to rotation of the enzyme were observed, with the central stalk’s ε subunit in an extended autoinhibitory conformation in all three states. The Fo motor comprises of seven transmembrane helices and a decameric c-ring and invaginations on either side of the membrane indicate the entry and exit channels for protons. The proton translocating subunit contains near parallel helices inclined by ~30° to the membrane, a feature now synonymous with rotary ATPases. For the first time in this rotary ATPase subtype, the peripheral stalk is resolved over its entire length of the complex, revealing the F1 attachment points and a coiled-coil that bifurcates toward the membrane with its helices separating to embrace subunit a from two sides.
DOI: 10.7554/eLife.21598
Rights: © Sobti et al. This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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