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  F1-ATPase conformational cycle from simultaneous single-molecule FRET and rotation measurements

Sugawa, M., Okazaki, K.-i., Kobayashi, M., Matsui, T., Hummer, G., Masaike, T., et al. (2016). F1-ATPase conformational cycle from simultaneous single-molecule FRET and rotation measurements. Proceedings of the National Academy of Sciences of the United States of America, 113(21), E2916-E2924. doi:10.1073/pnas.1524720113.

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 Creators:
Sugawa, Mitsuhiro1, Author
Okazaki, Kei-ichi2, Author              
Kobayashi, Masaru1, Author
Matsui, Takashi1, Author
Hummer, Gerhard2, Author              
Masaike, Tomoko1, 3, 4, Author
Nishizaka, Takayuki1, Author
Affiliations:
1aDepartment of Physics, Faculty of Science, Gakushuin University, Tokyo 171-8588, Japan, ou_persistent22              
2Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068292              
3Department of Applied Biological Science, Tokyo University of Science, Chiba-ken 278-8510, Japan, ou_persistent22              
4Precursory Research for Embryonic Science and Technology, Japan Science and Technology Agency, Saitama 332-0012, Japan, ou_persistent22              

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Free keywords: F1-ATPase; single molecule; FRET; principal component analysis
 Abstract: Despite extensive studies, the structural basis for the mechanochemical coupling in the rotary molecular motor F1-ATPase (F1) is still incomplete. We performed single-molecule FRET measurements to monitor conformational changes in the stator ring-α3β3, while simultaneously monitoring rotations of the central shaft-γ. In the ATP waiting dwell, two of three β-subunits simultaneously adopt low FRET nonclosed forms. By contrast, in the catalytic intermediate dwell, two β-subunits are simultaneously in a high FRET closed form. These differences allow us to assign crystal structures directly to both major dwell states, thus resolving a long-standing issue and establishing a firm connection between F1 structure and the rotation angle of the motor. Remarkably, a structure of F1 in an ε-inhibited state is consistent with the unique FRET signature of the ATP waiting dwell, while most crystal structures capture the structure in the catalytic dwell. Principal component analysis of the available crystal structures further clarifies the five-step conformational transitions of the αβ-dimer in the ATPase cycle, highlighting the two dominant modes: the opening/closing motions of β and the loosening/tightening motions at the αβ-interface. These results provide a new view of tripartite coupling among chemical reactions, stator conformations, and rotary angles in F1-ATPase.

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Language(s): eng - English
 Dates: 2016-04-152016-05-022016-05-24
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.1524720113
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : Proc. Acad. Sci. USA
  Other : Proc. Acad. Sci. U.S.A.
  Abbreviation : PNAS
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 113 (21) Sequence Number: - Start / End Page: E2916 - E2924 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230