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Structural mechanism of the ATP-induced dissociation of rigor myosin from actin.

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 ? 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.

SUBMITTER: Kuhner S

PROVIDER: S-EPMC3093495 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature

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Structural mechanism of the ATP-induced dissociation of rigor myosin from actin.

Kühner Sebastian S Fischer Stefan S

Proceedings of the National Academy of Sciences of the United States of America 20110425 19

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 ...[more]

PMID: 21518908

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