A structural model for actin-induced nucleotide release in myosin |
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Authors: | Reubold Thomas F Eschenburg Susanne Becker Andreas Kull F Jon Manstein Dietmar J |
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Institution: | Abteilung Biophysik, Max-Planck Institut für medizinische Forschung, Jahnstr. 29, D-69120 Heidelberg, Germany. |
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Abstract: | Myosins are molecular motor proteins that harness the chemical energy stored in ATP to produce directed force along actin filaments. Complex communication pathways link the catalytic nucleotide-binding region, the structures responsible for force amplification and the actin-binding domain of myosin. We have crystallized the nucleotide-free motor domain of myosin II in a new conformation in which switch I and switch II, conserved loop structures involved in nucleotide binding, have moved away from the nucleotide-binding pocket. These movements are linked to rearrangements of the actin-binding region, which illuminate a previously unobserved communication pathway between the nucleotide-binding pocket and the actin-binding region, explain the reciprocal relationship between actin and nucleotide affinity and suggest a new mechanism for product release in myosin family motors. |
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