3-Dimensional Imaging of Motor Proteins Provides New Insights to Molecular Mechanics of Cell Motility, Muscle Contraction
Scientists from the Burnham Institute for Medical Research and the University of Vermont have captured the first 3-dimensional (3D) atomic-resolution images of the motor protein myosin V as it "walks" along other proteins, revealing new structural insights that advance the current model of protein motility and muscle contraction. The culmination of four years of work, this collaboration among biochemists and structural biologists was selected as the cover story for the September issue of the scientific journal Molecular Cell.
The Burnham team, led by Dorit Hanein, Ph.D., was the first to reveal the 3D representation of myosin V "walking" along actin filament, a key protein involved in motility and muscle contraction. Using electron-cryo microscopy to take 3D snapshots of myosin V and actin interacting, researchers were able to see myosin V moving along the actin substrate in a "natural state." Previous 2D models have been based on staining or other treatment of the myosin that might alter the complexs natural mechanism of action.
Nancy Beddingfield | EurekAlert!
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