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| | ==Crystal Structure of Apoenzyme Alpha-kinase Domain of Myosin-II Heavy Chain Kinase A== | | ==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=''> | + | <StructureSection load='5e4h' size='340' side='right'caption='[[5e4h]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5e4h]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11735 Atcc 11735]. 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> | + | <table><tr><td colspan='2'>[[5e4h]] is a 8 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=5E4H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PHD:ASPARTYL+PHOSPHATE'>PHD</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5e4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e4h OCA], [https://pdbe.org/5e4h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e4h RCSB], [https://www.ebi.ac.uk/pdbsum/5e4h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e4h ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mhkA, mhckA, DDB_G0291231 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 ATCC 11735])</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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e4h ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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. | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5e4h" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5e4h" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Myosin 3D Structures|Myosin 3D Structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 11735]] | + | [[Category: Dictyostelium discoideum]] |
| - | [[Category: Cote, G P]] | + | [[Category: Large Structures]] |
| - | [[Category: Jia, Z]] | + | [[Category: Cote GP]] |
| - | [[Category: Ye, Q]] | + | [[Category: Jia Z]] |
| - | [[Category: Alpha kinase]] | + | [[Category: Ye Q]] |
| - | [[Category: Epk domain fold]]
| + | |
| - | [[Category: Transferase]]
| + | |
| 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 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ye Q, Yang Y, van Staalduinen L, Crawley SW, Liu L, Brennan S, Cote GP, Jia Z. Structure of the Dictyostelium Myosin-II Heavy Chain Kinase A (MHCK-A) alpha-kinase domain apoenzyme reveals a novel autoinhibited conformation. Sci Rep. 2016 May 23;6:26634. doi: 10.1038/srep26634. PMID:27211275 doi:http://dx.doi.org/10.1038/srep26634
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