5e4h: Difference between revisions
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==Crystal Structure of Apoenzyme Alpha-kinase Domain of Myosin-II Heavy Chain Kinase A== | |||
<StructureSection load='5e4h' size='340' side='right' caption='[[5e4h]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5e4h]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E4H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E4H FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PHD:ASPARTYL+PHOSPHATE'>PHD</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lla|3lla]], [[3lmh|3lmh]], [[3lkm|3lkm]], [[3lmi|3lmi]], [[3pdt|3pdt]], [[4zme|4zme]], [[4zmf|4zmf]], [[4zs4|4zs4]], [[5e9e|5e9e]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Myosin_heavy-chain]_kinase [Myosin heavy-chain] kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.7 2.7.11.7] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5e4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e4h OCA], [http://pdbe.org/5e4h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e4h RCSB], [http://www.ebi.ac.uk/pdbsum/5e4h PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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 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<ref>PMID:27211275</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5e4h" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cote, G P]] | |||
[[Category: Jia, Z]] | [[Category: Jia, Z]] | ||
[[Category: Ye, Q]] | [[Category: Ye, Q]] | ||
[[Category: | [[Category: Alpha kinase]] | ||
[[Category: Epk domain fold]] | |||
[[Category: Transferase]] | |||
Revision as of 18:21, 20 June 2016
Crystal Structure of Apoenzyme Alpha-kinase Domain of Myosin-II Heavy Chain Kinase ACrystal Structure of Apoenzyme Alpha-kinase Domain of Myosin-II Heavy Chain Kinase A
Structural highlights
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 PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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