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

@article{Yan2000CrystalSO,
  title={Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases.},
  author={Yuan Ji Yan and Nickolai A. Barlev and Randall H. Haley and Shelley L Berger and Ronen Marmorstein},
  journal={Molecular cell},
  year={2000},
  volume={6 5},
  pages={
          1195-205
        }
}
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… CONTINUE READING
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