6z7t

Nucleotide-free Myosin-II motor domain

spinqualitylabelsall models 6z7t, resolution 1.88Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6z7t is a 2 chain structure with sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.88Å Ligands: EDO, GOL, MG, PEG, PGE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MYS2_DICDI Myosin is a protein that binds to actin and has ATPase activity that is activated by actin. Publication Abstract from PubMed The motor protein myosin drives a wide range of cellular and muscular functions by generating directed movement and force, fueled through adenosine triphosphate (ATP) hydrolysis. Release of the hydrolysis product adenosine diphosphate (ADP) is a fundamental and regulatory process during force production. However, details about the molecular mechanism accompanying ADP release are scarce due to the lack of representative structures. Here we solved a novel blebbistatin-bound myosin conformation with critical structural elements in positions between the myosin pre-power stroke and rigor states. ADP in this structure is repositioned towards the surface by the phosphate-sensing P-loop, and stabilized in a partially unbound conformation via a salt-bridge between Arg131 and Glu187. A 5 A rotation separates the mechanical converter in this conformation from the rigor position. The crystallized myosin structure thus resembles a conformation towards the end of the two-step power stroke, associated with ADP release. Computationally reconstructing ADP release from myosin by means of molecular dynamics simulations further supported the existence of an equivalent conformation along the power stroke that shows the same major characteristics in the myosin motor domain as the resolved blebbistatin-bound myosin-II.ADP crystal structure, and identified a communication hub centered on Arg232 that mediates chemomechanical energy transduction. Structural and Computational Insights into a Blebbistatin-Bound Myosin*ADP Complex with Characteristics of an ADP-Release Conformation along the Two-Step Myosin Power Stoke.,Ewert W, Franz P, Tsiavaliaris G, Preller M Int J Mol Sci. 2020 Oct 8;21(19). pii: ijms21197417. doi: 10.3390/ijms21197417. PMID:33049993 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Myosin 3D Structures

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