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==Crystal Structure of the Alpha-kinase Domain of Myosin-II Heavy Chain Kinase A in Complex with Adenosine== | ==Crystal Structure of the Alpha-kinase Domain of Myosin-II Heavy Chain Kinase A in Complex with Adenosine== | ||
<StructureSection load='4zme' size='340' side='right' caption='[[4zme]], [[Resolution|resolution]] 1.98Å' scene=''> | <StructureSection load='4zme' size='340' side='right'caption='[[4zme]], [[Resolution|resolution]] 1.98Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4zme]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZME OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4zme]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZME OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZME FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PHD:ASPARTYL+PHOSPHATE'>PHD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
< | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4zme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zme OCA], [https://pdbe.org/4zme PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zme RCSB], [https://www.ebi.ac.uk/pdbsum/4zme PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zme ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/MHCKA_DICDI 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. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The alpha-kinases are a widely expressed family of serine/threonine protein kinases that exhibit no sequence identity with conventional eukaryotic protein kinases. In this report we provide new information on the catalytic properties of the alpha-kinase domain of Dictyostelium myosin-II heavy chain kinase-A (termed A-CAT). Crystallization of A-CAT in the presence of MgATP yielded structures with AMP or adenosine in the catalytic cleft together with a phosphorylated Asp766 residue. The results show that the beta- and alpha-phosphoryl groups are transferred either directly or indirectly to the catalytically essential Asp766. Biochemical assays confirmed that A-CAT hydrolyzed ATP, ADP and AMP with kcat values of 1.9, 0.6 and 0.32 min-1, respectively, and showed that A-CAT can use ADP to phosphorylate peptides and proteins. Binding assays using fluorescent 2/3-O-(N-Methyl-anthraniloyl) analogs of ATP and ADP yielded Kd values for ATP, ADP, AMP and adenosine of 20, 60, 160 and 45 micromole, respectively. Site-directed mutagenesis showed that Glu713, Leu716 and Lys645, all of which interact with the adenine base, were critical for nucleotide binding. Mutation of the highly conserved Gln758, which chelates a nucleotide-associated Mg2+ ion, eliminated catalytic activity, whereas loss of the highly conserved Lys722 and Arg592 decreased kcat for kinase and ATPase activities by 3-6-fold. Mutation of Asp663 impaired kinase activity to a much greater extent than ATPase, indicating a specific role in peptide substrate binding, whereas mutation of Gln768 doubled ATPase activity, suggesting that it may act to exclude water from the active site. | |||
Characterization of the Catalytic and Nucleotide Binding Properties of the Alpha-kinase domain of Dictyostelium Myosin-II Heavy Chain Kinase A.,Yang Y, Ye Q, Jia Z, Cote GP J Biol Chem. 2015 Aug 10. pii: jbc.M115.672410. PMID:26260792<ref>PMID:26260792</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4zme" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Dictyostelium discoideum]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Jia Z]] | ||
[[Category: | [[Category: Ye Q]] | ||