5i4e | pdb_00005i4e

Crystal Structure of Human Nonmuscle Myosin 2C motor domain

spinqualitylabelsall models 5i4e, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5i4e is a 1 chain structure with sequence from Dictyostelium discoideum and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.25Å Ligands: AOV, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease MYH14_HUMAN Peripheral neuropathy-myopathy-hoarseness-hearing loss syndrome;Autosomal dominant non-syndromic sensorineural deafness type DFNA. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. Function ACTNA_DICDI F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Increases the actin-stimulated ATPase activity of myosin. Involved in vegetative cell growth, phagocytosis, motility and development, probably through stabilization of the actin network in the cortical cytoskeleton. MYH14_HUMAN Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Publication Abstract from PubMed Despite a generic, highly conserved motor domain, ATP turnover kinetics and their activation by F-actin vary greatly between myosin-2 isoforms. Here, we present a 2.25 A pre-powerstroke state (ADPVO4) crystal structure of the human nonmuscle myosin-2C motor domain, one of the slowest myosins characterized. In combination with integrated mutagenesis, ensemble-solution kinetics, and molecular dynamics simulation approaches, the structure reveals an allosteric communication pathway that connects the distal end of the motor domain with the active site. Disruption of this pathway by mutation of hub residue R788, which forms the center of a cluster of interactions connecting the converter, the SH1-SH2 helix, the relay helix, and the lever, abolishes nonmuscle myosin-2 specific kinetic signatures. Our results provide insights into structural changes in the myosin motor domain that are triggered upon F-actin binding and contribute critically to the mechanochemical behavior of stress fibers, actin arcs, and cortical actin-based structures. Mechanistic insights into the active site and allosteric communication pathways in human nonmuscle myosin-2C.,Chinthalapudi K, Heissler SM, Preller M, Sellers JR, Manstein DJ Elife. 2017 Dec 19;6. pii: 32742. doi: 10.7554/eLife.32742. PMID:29256864 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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