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Literature summary for 2.3.1.48 extracted from

  • Jiang, J.; Lu, J.; Lu, D.; Liang, Z.; Li, L.; Ouyang, S.; Kong, X.; Jiang, H.; Shen, B.; Luo, C.
    Investigation of the acetylation mechanism by GCN5 histone acetyltransferase (2012), PLoS ONE, 7, e36660.
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
modeling of the initial complex between acetyltransferase Gcn5, acetyl-CoA and histone H3 and 20 ns molecular dynamics simulation. Glu80 acts as the general base for deprotonation of residue Lys171 from H3. Glu80, water180 and Lys171 form a proton-wire for the deprotonation process of Lys171. Both loop alpha7-beta7 and loop alpha1-alpha2 play a critical role in binding substrate H3 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q92830
-
-

Synonyms

Synonyms Comment Organism
Gcn5
-
 Homo sapiens
Kat2A
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 Homo sapiens