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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Pylypenko, Olena Wulf, Sarah F. Hofhaus, Goetz Houdusse, Anne M. Trabuco, Leonardo G. Fujita-becker, Setsuko Oster, Marco Ropars, Virginie Sweeney, H. Lee Schröder, Rasmus R. |
| Description | Author Affiliation: Wulf SF ( Cryo Electron Microscopy, CellNetworks, BioQuant, Universitätsklinikum Heidelberg, 69120 Heidelberg, Germany); Ropars V ( Structural Motility, Institut Curie, Paris Sciences et Lettres Research University, CNRS, UMR 144, F-75005, Paris, France); Fujita-Becker S ( Cryo Electron Microscopy, CellNetworks, BioQuant, Universitätsklinikum Heidelberg, 69120 Heidelberg, Germany); Oster M ( Cryo Electron Microscopy, CellNetworks, BioQuant, Universitätsklinikum Heidelberg, 69120 Heidelberg, Germany); Hofhaus G ( Cryo Electron Microscopy, CellNetworks, BioQuant, Universitätsklinikum Heidelberg, 69120 Heidelberg, Germany); Trabuco LG ( Protein Evolution, CellNetworks, BioQuant, Universität Heidelberg, 69120 Heidelberg, Germany); Pylypenko O ( Structural Motility, Institut Curie, Paris Sciences et Lettres Research University, CNRS, UMR 144, F-75005, Paris, France); Sweeney HL ( Department of Pharmacology & Therapeutics, University of Florida College of Medicine, Gainesville, FL 32610 anne.houdusse@curie.fr Lsweeney@ufl.edu rasmus.schroeder@bioquant.uni-heidelberg.de.); Houdusse AM ( Structural Motility, Institut Curie, Paris Sciences et Lettres Research University, CNRS, UMR 144, F-75005, Paris, France); Schröder RR ( Cryo Electron Microscopy, CellNetworks, BioQuant, Universitätsklinikum Heidelberg, 69120 Heidelberg, Germany); |
| Abstract | 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-Å 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 ß-sheet underlying the nucleotide pocket. The transition from the force-generating ADP state to Rigor requires a 9.5° rotation of the myosin lever arm, coupled to a ß-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. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 13 |
| Volume Number | 113 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2016-04-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Actins Metabolism Adenosine Diphosphate Myosin Type V Chemistry Binding Sites Cryoelectron Microscopy Crystallography, X-Ray Models, Molecular Molecular Dynamics Simulation Protein Conformation Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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