5e9e

Crystal Structure of the Alpha-kinase Domain of Myosin-II Heavy Chain Kinase A in Complex with AMP-PNP

spinqualitylabelsall models 5e9e, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5e9e 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 2.4Å Ligands: ANP, PO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MHCKA_DICDI Phosphorylates threonine in the C-terminal tail region of myosin II heavy chain. This phosphorylation is critical in regulating the assembly and disassembly of myosin II filament. Requires autophosphorylation for activity. Publication Abstract from PubMed The alpha-kinases are a family of a typical protein kinases present in organisms ranging from protozoa to mammals. Here we report an autoinhibited conformation for the alpha-kinase domain of Dictyostelium myosin-II heavy chain kinase A (MHCK-A) in which nucleotide binding to the catalytic cleft, located at the interface between an N-terminal and C-terminal lobe, is sterically blocked by the side chain of a conserved arginine residue (Arg592). Previous alpha-kinase structures have shown that an invariant catalytic aspartic acid residue (Asp766) is phosphorylated. Unexpectedly, in the autoinhibited conformation the phosphoryl group is transferred to the adjacent Asp663, creating an interaction network that stabilizes the autoinhibited state. The results suggest that Asp766 phosphorylation may play both catalytic and regulatory roles. The autoinhibited structure also provides the first view of a phosphothreonine residue docked into the phospho-specific allosteric binding site (Pi-pocket) in the C-lobe of the alpha-kinase domain. Structure of the Dictyostelium Myosin-II Heavy Chain Kinase A (MHCK-A) alpha-kinase domain apoenzyme reveals a novel autoinhibited conformation.,Ye Q, Yang Y, van Staalduinen L, Crawley SW, Liu L, Brennan S, Cote GP, Jia Z Sci Rep. 2016 May 23;6:26634. doi: 10.1038/srep26634. PMID:27211275 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Myosin 3D Structures

Proteopedia Page Contributors and Editors (what is this?)

OCA