Structural Mechanism of the ATP-induced Dissociation of Rigor Myosin from Actin

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 2011 Apr 27

PMID 21518908

Citations 16

Authors

Sebastian Kuhner

Stefan Fischer

Affiliations

Soon will be listed here.

Abstract

Myosin is a true nanomachine, which produces mechanical force from ATP hydrolysis by cyclically interacting with actin filaments in a four-step cycle. The principle underlying each step is that structural changes in separate regions of the protein must be mechanically coupled. The step in which myosin dissociates from tightly bound actin (the rigor state) is triggered by the 30 Å distant binding of ATP. Large conformational differences between the crystal structures make it difficult to perceive the coupling mechanism. Energetically accessible transition pathways computed at atomic detail reveal a simple coupling mechanism for the reciprocal binding of ATP and actin.

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