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Molecular simulation and modeling of functional dynamics in biomolecular motor
Date : Thursday, August 3rd, 2017 16:00 - 17:00 Place : Seminar Room 5 (A615), 6th Floor, ISSP Lecturer : Prof. Kei-ichi Okazaki Affiliation : Department of Theoretical and Computational Molecular Science, Institute for Molecular Science Committee Chair : Hiroshi NOGUCHI (ex.63265)

F0F1 ATP synthase is one of the most important biomolecules, synthesizing most of ATP in the cell. Especially the catalytic part, F1-ATPase, has been extensively studied by both crystallography and single-molecule experiments, revealing atomistic structures and detailed mechanochemical coupling scheme, respectively. However, connection between these two aspects are not well established: structural basis of the functional cycle has been controversial. We previously performed systematic structural analysis [1] and molecular dynamics simulations [2] to clarify the connection. We have been recently working on multiscale dynamics of this rotary motor, to understand how the ATP hydrolysis reaction drives the large-scale rotational motion. For the whole F0F1 ATP synthase, we built a simple viscoelastic model to explain symmetry mismatch between F0 and F1 motors [3].

[1] Mitsuhiro Sugawa, Kei-ichi Okazaki, et al. (2016) “F1-ATPase conformational cycle from simultaneous single-molecule FRET and rotation measurements” Proc. Natl. Acad. Sci. USA, 113 (21): E2916-E2924
[2] Kei-ichi Okazaki and Gerhard Hummer (2013) “Phosphate release coupled to rotary motion of F1-ATPase” Proc. Natl. Acad. Sci. USA, 110 (41): 16468-16473
[3] Kei-ichi Okazaki and Gerhard Hummer (2015) “Elasticity, friction, and pathway of γ-subunit rotation in F0F1-ATP synthase” Proc. Natl. Acad. Sci. USA, 112 (34) 10720-10725

(Published on: Wednesday July 26th, 2017)