The Structural Basis for the Large Powerstroke of Myosin VI
| Autor: | Paola Llinas, Julie Ménétrey, H. Lee Sweeney, Anne Houdusse, Monalisa Mukherjea |
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| Rok vydání: | 2007 |
| Předmět: |
Models
Molecular business.product_category Protein Conformation Swine PROTEINS macromolecular substances Biology Crystallography X-Ray General Biochemistry Genetics and Molecular Biology Myosin head Protein structure Myosin Animals Actin Lever Myosin Heavy Chains Extramural Biochemistry Genetics and Molecular Biology(all) Molecular Motor Proteins Myosin Subfragments Structural protein Anatomy Actin Cytoskeleton Biophysics business Large size |
| Zdroj: | Cell. 131(2):300-308 |
| ISSN: | 0092-8674 |
| DOI: | 10.1016/j.cell.2007.08.027 |
| Popis: | SummaryDue to a unique addition to the lever arm-positioning region (converter), class VI myosins move in the opposite direction (toward the minus-end of actin filaments) compared to other characterized myosin classes. However, the large size of the myosin VI lever arm swing (powerstroke) cannot be explained by our current view of the structural transitions that occur within the myosin motor. We have solved the crystal structure of a fragment of the myosin VI motor in the structural state that represents the starting point for movement on actin; the pre-powerstroke state. Unexpectedly, the converter itself rearranges to achieve a conformation that has not been seen for other myosins. This results in a much larger powerstroke than is achievable without the converter rearrangement. Moreover, it provides a new mechanism that could be exploited to increase the powerstroke of yet to be characterized plus-end-directed myosin classes. |
| Databáze: | OpenAIRE |
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