4l79
Crystal Structure of nucleotide-free Myosin 1b residues 1-728 with bound CalmodulinCrystal Structure of nucleotide-free Myosin 1b residues 1-728 with bound Calmodulin
Structural highlights
FunctionMYO1B_RAT Motor protein that may participate in process critical to neuronal development and function such as cell migration, neurite outgrowth and vesicular transport (By similarity). Publication Abstract from PubMedMyosins are molecular motors that power diverse cellular processes, such as rapid organelle transport, muscle contraction, and tension-sensitive anchoring. The structural adaptations in the motor that allow for this functional diversity are not known, due, in part, to the lack of high-resolution structures of highly tension-sensitive myosins. We determined a 2.3-A resolution structure of apo-myosin-Ib (Myo1b), which is the most tension-sensitive myosin characterized. We identified a striking unique orientation of structural elements that position the motor's lever arm. This orientation results in a cavity between the motor and lever arm that holds a 10-residue stretch of N-terminal amino acids, a region that is divergent among myosins. Single-molecule and biochemical analyses show that the N terminus plays an important role in stabilizing the post power-stroke conformation of Myo1b and in tuning the rate of the force-sensitive transition. We propose that this region plays a general role in tuning the mechanochemical properties of myosins. A vertebrate myosin-I structure reveals unique insights into myosin mechanochemical tuning.,Shuman H, Greenberg MJ, Zwolak A, Lin T, Sindelar CV, Dominguez R, Ostap EM Proc Natl Acad Sci U S A. 2014 Feb 11;111(6):2116-21. doi:, 10.1073/pnas.1321022111. Epub 2014 Jan 27. PMID:24469830[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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