7shq: Difference between revisions
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New page: '''Unreleased structure''' The entry 7shq is ON HOLD Authors: Description: Category: Unreleased Structures |
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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]], [[Resolution|resolution]] 2.34Å' scene=''> | |||
== Structural highlights == | |||
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.34Å</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> | |||
== 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-2K(TR)). This structure, which represents the activated T348-phosphorylated state of eEF-2K(TR), 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> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7shq" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Calmodulin 3D structures|Calmodulin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Dalby KN]] | |||
[[Category: Ghose R]] | |||
[[Category: Isiorho EA]] | |||
[[Category: Jeruzalmi D]] | |||
[[Category: Piserchio A]] | |||