A structural model for actin-induced nucleotide release in myosin Export

@article{citeulike:6043175, 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.}, author = {Reubold, Thomas F. and Eschenburg, Susanne and Becker, Andreas and Kull, F. Jon and Manstein, Dietmar J.}, citeulike-article-id = {6043175}, citeulike-linkout-0 = {http://dx.doi.org/10.1038/nsb987}, citeulike-linkout-1 = {http://dx.doi.org/10.1038/nsb987}, day = {21}, doi = {10.1038/nsb987}, journal = {Nature Structural \& Molecular Biology}, keywords = {structures}, month = {September}, number = {10}, pages = {826--830}, posted-at = {2009-10-30 14:41:08}, priority = {2}, publisher = {Nature Publishing Group}, title = {A structural model for actin-induced nucleotide release in myosin}, url = {http://dx.doi.org/10.1038/nsb987}, volume = {10}, year = {2003} }

TY - JOUR ID - citeulike:6043175 L3 - citeulike-article-id:6043175 N2 - 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. IS - 10 JF - Nature Structural & Molecular Biology EP - 830 TI - A structural model for actin-induced nucleotide release in myosin PB - Nature Publishing Group VL - 10 SP - 826 KW - structures AU - Reubold, Thomas AU - Eschenburg, Susanne AU - Becker, Andreas AU - Kull, Jon AU - Manstein, Dietmar PY - 2003/09/21/ UR - http://dx.doi.org/10.1038/nsb987 ER -