4e7s | pdb_00004e7s

Myosin VI D23R I24R R569E (MD) pre-powerstroke state

spinqualitylabelsall models 4e7s, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4e7s is a 2 chain structure with sequence from Sus scrofa. 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: ADP, GOL, MG, PO4, VO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F1RQI7_PIG Publication Abstract from PubMed Myosin VI is the only known reverse-direction myosin motor. It has an unprecedented means of amplifying movements within the motor involving rearrangements of the converter subdomain at the C terminus of the motor and an unusual lever arm projecting from the converter. While the average step size of a myosin VI dimer is 30-36 nm, the step size is highly variable, presenting a challenge to the lever arm mechanism by which all myosins are thought to move. Herein, we present structures of myosin VI that reveal regions of compliance that allow an uncoupling of the lead head when movement is modeled on actin. The location of the compliance restricts the possible actin binding sites and predicts the observed stepping behavior. The model reveals that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. Processive Steps in the Reverse Direction Require Uncoupling of the Lead Head Lever Arm of Myosin VI.,Menetrey J, Isabet T, Ropars V, Mukherjea M, Pylypenko O, Liu X, Perez J, Vachette P, Sweeney HL, Houdusse AM Mol Cell. 2012 Aug 29. PMID:22940248 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Myosin 3D Structures

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