7shq
From Proteopedia
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| - | ==== | + | ==Structure of a functional construct of eukaryotic elongation factor 2 kinase in complex with calmodulin.== |
| - | <StructureSection load='7shq' size='340' side='right'caption='[[7shq]]' scene=''> | + | <StructureSection load='7shq' size='340' side='right'caption='[[7shq]], [[Resolution|resolution]] 2.34Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7shq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SHQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SHQ FirstGlance]. <br> |
| - | </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=7shq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7shq OCA], [https://pdbe.org/7shq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7shq RCSB], [https://www.ebi.ac.uk/pdbsum/7shq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7shq ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=7shq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7shq OCA], [https://pdbe.org/7shq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7shq RCSB], [https://www.ebi.ac.uk/pdbsum/7shq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7shq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/EF2K_HUMAN EF2K_HUMAN]] Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced.<ref>PMID:14709557</ref> <ref>PMID:9144159</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Translation is a tightly regulated process that ensures optimal protein quality and enables adaptation to energy/nutrient availability. The alpha-kinase eukaryotic elongation factor 2 kinase (eEF-2K), a key regulator of translation, specifically phosphorylates the guanosine triphosphatase eEF-2, thereby reducing its affinity for the ribosome and suppressing the elongation phase of protein synthesis. eEF-2K activation requires calmodulin binding and autophosphorylation at the primary stimulatory site, T348. Biochemical studies predict a calmodulin-mediated activation mechanism for eEF-2K distinct from other calmodulin-dependent kinases. Here, we resolve the atomic details of this mechanism through a 2.3-A crystal structure of the heterodimeric complex of calmodulin and the functional core of eEF-2K (eEF-2KTR). This structure, which represents the activated T348-phosphorylated state of eEF-2KTR, highlights an intimate association of the kinase with the calmodulin C-lobe, creating an "activation spine" that connects its amino-terminal calmodulin-targeting motif to its active site through a conserved regulatory element. | ||
| + | |||
| + | Structural basis for the calmodulin-mediated activation of eukaryotic elongation factor 2 kinase.,Piserchio A, Isiorho EA, Long K, Bohanon AL, Kumar EA, Will N, Jeruzalmi D, Dalby KN, Ghose R Sci Adv. 2022 Jul 8;8(27):eabo2039. doi: 10.1126/sciadv.abo2039. Epub 2022 Jul 6. PMID:35857468<ref>PMID:35857468</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7shq" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Dalby KN]] |
| + | [[Category: Ghose R]] | ||
| + | [[Category: Isiorho EA]] | ||
| + | [[Category: Jeruzalmi D]] | ||
| + | [[Category: Piserchio A]] | ||
Revision as of 03:52, 8 September 2022
Structure of a functional construct of eukaryotic elongation factor 2 kinase in complex with calmodulin.
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