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Structure paper

TitleThe catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate.
Journal, issue, pagesNat. Struct. Biol., Vol. 9, Page 862-869, Year 2002
Publish dateAug 27, 2002 (structure data deposition date)
AuthorsYan, Y. / Harper, S. / Speicher, D.W. / Marmorstein, R.
External linksNat. Struct. Biol. / PubMed:12368900
MethodsX-ray diffraction
Resolution2.26 - 2.5 Å
Structure data

PDB-1mj9:
Crystal structure of yeast Esa1(C304S) mutant complexed with Coenzyme A
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-1mja:
Crystal structure of yeast Esa1 histone acetyltransferase domain complexed with acetyl coenzyme A
Method: X-RAY DIFFRACTION / Resolution: 2.26 Å

PDB-1mjb:
Crystal structure of yeast Esa1 histone acetyltransferase E338Q mutant complexed with acetyl coenzyme A
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-COA:
COENZYME A

ChemComp-HOH:
WATER

ChemComp-ACO:
ACETYL COENZYME *A

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsTRANSFERASE / Esa1 / HAT / Histone acetyltransferase / MYST / histone acetyltransferases

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