1FY7

CRYSTAL STRUCTURE OF YEAST ESA1 HISTONE ACETYLTRANSFERASE DOMAIN COMPLEXED WITH COENZYME A

Summary for 1FY7

• Entry DOI: 10.2210/pdb1fy7/pdb
• Descriptor: ESA1 HISTONE ACETYLTRANSFERASE, SODIUM ION, COENZYME A, ... (4 entities in total)
• Functional Keywords: histone acetyltransferase, coenzyme a, transferase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 34162.94

Authors

Yan, Y.,Barlev, N.A.,Haley, R.H.,Berger, S.L.,Marmorstein, R. (deposition date: 2000-09-28, release date: 2000-11-29, Last modification date: 2024-02-07)

Primary citation

Yan, Y.,Barlev, N.A.,Haley, R.H.,Berger, S.L.,Marmorstein, R.
Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases.
Mol.Cell, 6:1195-1205, 2000

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.

PubMed: 11106757
DOI: 10.1016/S1097-2765(00)00116-7

Experimental method

X-RAY DIFFRACTION (2 Å)