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'''Unreleased structure'''


The entry 9pcq is ON HOLD  until Paper Publication
==Phosphorylation of a Conserved Aspartate at the Eukaryotic Elongation Factor 2 Kinase Catalytic Site==
<StructureSection load='9pcq' size='340' side='right'caption='[[9pcq]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9pcq]] 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=9PCQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9PCQ 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9pcq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9pcq OCA], [https://pdbe.org/9pcq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9pcq RCSB], [https://www.ebi.ac.uk/pdbsum/9pcq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9pcq 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 ==
Eukaryotic elongation factor 2 kinase (eEF-2K) is a member of the alpha-kinase family of atypical serine/threonine kinases. eEF-2K, the only calmodulin-activated alpha-kinase, phosphorylates the ribosome-associated GTPase, eukaryotic elongation factor 2 (eEF-2), suppressing translational elongation. alpha-kinases, including eEF-2K, possess catalytic site geometries that are distinct from those of typical kinases, suggesting possible divergence in their phospho-transfer mechanisms. Unlike typical protein kinases, where chemistry is known to proceed through a sequential mechanism involving a ternary kinase-substrate-ATP*Mg(2+) complex, the nature of the chemical step catalyzed by alpha-kinases remains poorly defined. Here, multiple orthogonal lines of evidence, including a crystal structure and solution-state mass spectrometry data, suggest phosphorylation of a catalytically essential aspartate residue (D284) at the eEF-2K active site. Previous crystallographic evidence of the presence of a phospho-aspartate at an equivalent position (D766) in the related Dictyostelium alpha-kinase MHCK-A strongly suggests that this species represents a conserved active-site feature in alpha-kinase family members, despite their disparate modes of activation. This observation, together with existing kinetics data on eEF-2K, raises the possibility that phospho-transfer chemistry in alpha-kinases occurs via an ordered stepwise mechanism involving a phospho-enzyme intermediate, contrasting with typical protein kinases.


Authors: Piserchio, A., Isiorho, E.A., Dalby, K., Ghose, R.
Phosphorylation of a conserved aspartate in the catalytic site of eukaryotic elongation factor 2 kinase.,Piserchio A, Isiorho EA, Abzalimov R, Dalby KN, Ghose R Protein Sci. 2026 Jan;35(1):e70442. doi: 10.1002/pro.70442. PMID:41432361<ref>PMID:41432361</ref>


Description: Phosphorylation of a Conserved Aspartate at the Eukaryotic Elongation Factor 2 Kinase Catalytic Site
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Dalby, K]]
<div class="pdbe-citations 9pcq" style="background-color:#fffaf0;"></div>
[[Category: Piserchio, A]]
== References ==
[[Category: Isiorho, E.A]]
<references/>
[[Category: Ghose, R]]
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Dalby K]]
[[Category: Ghose R]]
[[Category: Isiorho EA]]
[[Category: Piserchio A]]
Retrieved from "https://proteopedia.org/9pcq"