1FY7

Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases.

(2000) Mol Cell 6: 1195-1205

• PubMed: 11106757 Search on PubMed
• DOI: https://doi.org/10.1016/s1097-2765(00)00116-7
• Primary Citation of Related Structures:  
  1FY7


• PubMed Abstract: 
  

  Esa1 is the catalytic subunit of the NuA4 histone acetylase (HAT) complex that acetylates histone H4, and it is a member of the MYST family of HAT proteins that includes the MOZ oncoprotein and the HIV-1 Tat interacting protein Tip60. Here we report the X-ray crystal structure of the HAT domain of Esa1 bound to coenzyme A and investigate the protein's catalytic mechanism. Our data reveal that Esa1 contains a central core domain harboring a putative catalytic base, and flanking domains that are implicated in histone binding. Comparisons with the Gcn5/PCAF and Hat1 proteins suggest a unified mechanism of catalysis and histone binding by HAT proteins, whereby a structurally conserved core domain mediates catalysis, and sequence variability within a structurally related N- and C-terminal scaffold determines substrate specificity.

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Organizational Affiliation: 

The Wistar Institute University of Pennsylvania, Philadelphia, PA 19104, USA.