2mys

MYOSIN SUBFRAGMENT-1, ALPHA CARBON COORDINATES ONLY FOR THE TWO LIGHT CHAINS

spinqualitylabelsall models 2mys, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mys is a 3 chain structure with sequence from Gallus gallus. This structure supersedes the now removed PDB entry 1mys. The June 2001 RCSB PDB Molecule of the Month feature on Myosin by David S. Goodsell is 10.2210/rcsb_pdb/mom_2001_6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: MG, MLY, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MYSS_CHICK Muscle contraction. Myosin is a protein that binds to F-actin and has ATPase activity that is activated by F-actin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Directed movement is a characteristic of many living organisms and occurs as a result of the transformation of chemical energy into mechanical energy. Myosin is one of three families of molecular motors that are responsible for cellular motility. The three-dimensional structure of the head portion of myosin, or subfragment-1, which contains both the actin and nucleotide binding sites, is described. This structure of a molecular motor was determined by single crystal x-ray diffraction. The data provide a structural framework for understanding the molecular basis of motility. Three-dimensional structure of myosin subfragment-1: a molecular motor.,Rayment I, Rypniewski WR, Schmidt-Base K, Smith R, Tomchick DR, Benning MM, Winkelmann DA, Wesenberg G, Holden HM Science. 1993 Jul 2;261(5117):50-8. PMID:8316857 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Myosin 3D Structures

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