1fy7 | pdb_00001fy7
CRYSTAL STRUCTURE OF YEAST ESA1 HISTONE ACETYLTRANSFERASE DOMAIN COMPLEXED WITH COENZYME A
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Overview
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.
About this Structure
1FY7 is a Single protein structure of sequence from Saccharomyces cerevisiae with NA and COA as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases., Yan Y, Barlev NA, Haley RH, Berger SL, Marmorstein R, Mol Cell. 2000 Nov;6(5):1195-205. PMID:11106757
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