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1MJA

Crystal structure of yeast Esa1 histone acetyltransferase domain complexed with acetyl coenzyme A

Summary for 1MJA
Entry DOI10.2210/pdb1mja/pdb
Related1FY7 1MJ9 1MJB
DescriptorEsa1 protein, COENZYME A (3 entities in total)
Functional Keywordsesa1, histone acetyltransferase, hat, myst, transferase
Biological sourceSaccharomyces cerevisiae (baker's yeast)
Total number of polymer chains1
Total formula weight34181.99
Authors
Yan, Y.,Harper, S.,Speicher, D.,Marmorstein, R. (deposition date: 2002-08-27, release date: 2002-10-30, Last modification date: 2024-11-20)
Primary citationYan, Y.,Harper, S.,Speicher, D.W.,Marmorstein, R.
The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate.
Nat.Struct.Biol., 9:862-869, 2002
Cited by
PubMed Abstract: Yeast ESA1 is a member of the MYST subfamily of histone acetyltransferases (HATs), which use acetyl-coenzyme A (CoA) to acetylate specific Lys residues within histones to regulate gene expression. The structure of an ESA1-CoA complex reveals structural similarity to the catalytic core of the GCN5/PCAF subfamily of HAT proteins. Here we report additional structural and functional studies on ESA1 that demonstrate that histone acetylation proceeds through an acetyl-cysteine enzyme intermediate. This Cys residue is strictly conserved within the MYST members, suggesting a common mode of catalysis by this HAT subfamily. However, this mode of catalysis differs dramatically from the GCN5/PCAF subfamily, which mediate direct nucleophilic attack of the acetyl-CoA cofactor by the enzyme-deprotonated substrate lysine of the histone. These results demonstrate that different HAT subfamilies can use distinct catalytic mechanisms, which have implications for their distinct biological roles and for the development of HAT-specific inhibitors.
PubMed: 12368900
DOI: 10.1038/nsb0902-638
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.26 Å)
Structure validation

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