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Structure paper

TitleADP enhances the allosteric activation of eukaryotic elongation factor 2 kinase by calmodulin.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 120, Page e2300902120-e2300902120, Year 2023
Publish dateDec 28, 2022 (structure data deposition date)
AuthorsPiserchio, A. / Long, K.J. / Browning, L.S. / Bohanon, A.L. / Isiorho, E.A. / Dalby, K.N. / Ghose, R.
External linksProc. Natl. Acad. Sci. USA / PubMed:37068230
MethodsX-ray diffraction
Resolution2.22 - 2.553 Å
Structure data

PDB-8fny:
Nucleotide-bound structure of a functional construct of eukaryotic elongation factor 2 kinase.
Method: X-RAY DIFFRACTION / Resolution: 2.22 Å

PDB-8fo6:
Nucleotide-free structure of a functional construct of eukaryotic elongation factor 2 kinase.
Method: X-RAY DIFFRACTION / Resolution: 2.553 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-ZN:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSLATION/Transferase / elongation factor 2 kinase / eEF2 / eEF2K / eEF-2K / Calmodulin / TRANSLATION / ATP / ADP / allostery / TRANSLATION-Transferase complex

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