Myosin and Other Energy-Transducing ATPases: Structural Dynamics Studied by Electron Paramagnetic Resonance.

Abstract:

:The objective of this article was to document the energy-transducing and regulatory interactions in supramolecular complexes such as motor, pump, and clock ATPases. The dynamics and structural features were characterized by motion and distance measurements using spin-labeling electron paramagnetic resonance (EPR) spectroscopy. In particular, we focused on myosin ATPase with actin-troponin-tropomyosin, neural kinesin ATPase with microtubule, P-type ion-motive ATPase, and cyanobacterial clock ATPase. Finally, we have described the relationships or common principles among the molecular mechanisms of various energy-transducing systems and how the large-scale thermal structural transition of flexible elements from one state to the other precedes the subsequent irreversible chemical reactions.

journal_name

Int J Mol Sci

authors

Arata T

doi

10.3390/ijms21020672

subject

Has Abstract

pub_date

2020-01-20 00:00:00

issue

2

issn

1422-0067

pii

ijms21020672

journal_volume

21

pub_type

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