The Structural Basis for the Large Powerstroke of Myosin VI

@article{citeulike:2234123, abstract = {Summary Due 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.}, author = {Menetrey, Julie and Llinas, Paola and Mukherjea, Monalisa and Sweeney, Lee H. and Houdusse, Anne }, citeulike-article-id = {2234123}, doi = {10.1016/j.cell.2007.08.027}, journal = {Cell}, keywords = {motor, myosin, xray-crystal-structure}, month = {October}, number = {2}, pages = {300--308}, posted-at = {2008-01-15 08:33:59}, priority = {2}, title = {The Structural Basis for the Large Powerstroke of Myosin VI}, url = {http://dx.doi.org/10.1016/j.cell.2007.08.027}, volume = {131}, year = {2007} }

TY - JOUR ID - citeulike:2234123 L3 - citeulike-article-id:2234123 TI - The Structural Basis for the Large Powerstroke of Myosin VI JF - Cell VL - 131 IS - 2 SP - 300 EP - 308 N2 - Summary Due 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. KW - motor KW - myosin KW - xray-crystal-structure AU - Menetrey, Julie AU - Llinas, Paola AU - Mukherjea, Monalisa AU - Sweeney, Lee AU - Houdusse, Anne PY - 2007/10/19/ UR - http://dx.doi.org/10.1016/j.cell.2007.08.027 ER -