1b7t | pdb_00001b7t

MYOSIN DIGESTED BY PAPAIN

spinqualitylabelsall models 1b7t, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1b7t is a 3 chain structure with sequence from Argopecten irradians. 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. Ligands: ADP, CA, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MYS_ARGIR] Muscle contraction. Myosin is a protein that binds to F-actin and has ATPase activity that is activated by F-actin. [MLE_ARGIR] In molluscan muscle, calcium regulation is associated with myosin rather than with actin. Muscle myosin contains two types of light chains: the catalytic light chain, essential for ATPase activity, and the regulatory light chain, a calcium-binding protein responsible for Ca(2+) dependent binding and Ca(2+) dependent Mg-ATPase activity. [MLR_ARGIR] In molluscan muscle, calcium regulation is associated with myosin rather than with actin. Muscle myosin contains two types of light chains: the catalytic light chain, essential for ATPase activity, and the regulatory light chain, a calcium-binding protein responsible for Ca(2+) dependent binding and Ca(2+) dependent Mg-ATPase activity. 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 The crystal structure of a proteolytic subfragment from scallop striated muscle myosin, complexed with MgADP, has been solved at 2.5 A resolution and reveals an unusual conformation of the myosin head. The converter and the lever arm are in very different positions from those in either the pre-power stroke or near-rigor state structures; moreover, in contrast to these structures, the SH1 helix is seen to be unwound. Here we compare the overall organization of the myosin head in these three states and show how the conformation of three flexible "joints" produces rearrangements of the four major subdomains in the myosin head with different bound nucleotides. We believe that this novel structure represents one of the prehydrolysis ("ATP") states of the contractile cycle in which the myosin heads stay detached from actin. Atomic structure of scallop myosin subfragment S1 complexed with MgADP: a novel conformation of the myosin head.,Houdusse A, Kalabokis VN, Himmel D, Szent-Gyorgyi AG, Cohen C Cell. 1999 May 14;97(4):459-70. PMID:10338210 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Myosin

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