期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 113, 期 13, 页码 E1844-E1852出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1516598113
关键词
molecular motor; force generation; transducer; myosin V
资金
- Ligue Nationale contre le Cancer
- CNRS
- Association pour la Recherche sur le Cancer subvention fixe
- National Institutes of Health/National Institute on Deafness and Other Communication Disorders [DC009100]
- National Institutes of Health (National Institute for General Medical Sciences) [P41-GM103311]
- Ministry of Science, Research and Arts and the Universities of the State of Baden-Wuerttemberg, Germany
- [ANR-2010-BLAN-1504-01]
- [ANR-13-BSV8-0019-01]
Molecular motors produce force when they interact with their cellular tracks. For myosin motors, the primary force-generating state has MgADP tightly bound, whereas myosin is strongly bound to actin. We have generated an 8-angstrom cryoEM reconstruction of this state for myosin V and used molecular dynamics flexed fitting for model building. We compare this state to the subsequent state on actin (Rigor). The ADP-bound structure reveals that the actin-binding cleft is closed, even though MgADP is tightly bound. This state is accomplished by a previously unseen conformation of the beta-sheet underlying the nucleotide pocket. The transition from the force-generating ADP state to Rigor requires a 9.5 degrees rotation of the myosin lever arm, coupled to a beta-sheet rearrangement. Thus, the structure reveals the detailed rearrangements underlying myosin force generation as well as the basis of strain-dependent ADP release that is essential for processive myosins, such as myosin V.
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