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Literature summary for 2.7.11.20 extracted from

  • Lee, K.; Alphonse, S.; Piserchio, A.; Tavares, C.D.; Giles, D.H.; Wellmann, R.M.; Dalby, K.N.; Ghose, R.
    Structural basis for the recognition of eukaryotic elongation factor 2 kinase by calmodulin (2016), Structure, 24, 1441-1451.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.11.20

Activating Compound

Activating Compound Comment Organism Structure
Calmodulin structural basis for the recognition of calmodulin by eukaryotic elongation factor 2 kinase, NMR spectrometric analysis, overview. The enzyme binds Ca2+-loaded CaM with high affinity largely through the CaM C lobe, but C-lobe-mediated interactions occur in a Ca2+-independent fashion. the lobe lacks bound calcium ions even under high calcium conditions. Conserved eEF-2K residue W85 anchors it to CaM by inserting into a deep hydrophobic cavity within the CaM C lobe. Mutation of residue W85 to S85 substantially weakens interactions between full-length eEF-2K and CaM in vitro and reduces eEF-2 phosphorylation in cells Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
recombinant coexpression of full-length human calmodulin (CaM), the predicted calmodulin-binding segment of human eEF-2K, residues 74-100 (eEF-2KCBD), and full-length eEF-2K Homo sapiens

Protein Variants

Protein Variants Comment Organism
W85S site-directed mutagenesis, Mutation of residue W85 to S85 substantially weakens interactions between full-length eEF-2K and CaM in vitro and reduces eEF-2 phosphorylation in cells Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Homo sapiens
Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + [elongation factor 2] Homo sapiens
-
 ADP + [elongation factor 2] phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens O00418
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant full-length human calmodulin (CaM), the predicted calmodulin-binding segment of human eEF-2K, residues 74-100 (eEF-2KCBD), and full-length eEF-2K Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + [elongation factor 2]
-
 Homo sapiens ADP + [elongation factor 2] phosphate
-
 ?

Synonyms

Synonyms Comment Organism
EEF-2K
-
 Homo sapiens
eukaryotic elongation factor 2 kinase
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Homo sapiens

General Information

General Information Comment Organism
evolution eukaryotic elongation factor 2 kinase is a member of the atypical alpha-kinase family Homo sapiens
malfunction mutation of the hydrophobic CaM anchor on eEF-2K disrupts its cellular activity. Mutation of residue W85 to S85 substantially weakens interactions between full-length eEF-2K and CaM in vitro and reduces eEF-2 phosphorylation in cells Homo sapiens
additional information solution structure of the Ca2+-CaM-eEF-2KCBD complex, structure analysis, NMR spectrometric analysis, detailed overview Homo sapiens
physiological function eukaryotic elongation factor 2 kinase (eEF-2K) phosphorylates eEF-2 leading to a decrease in global protein synthesis Homo sapiens