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TitleHat2p recognizes the histone H3 tail to specify the acetylation of the newly synthesized H3/H4 heterodimer by the Hat1p/Hat2p complex
Journal, issue, pagesGenes Dev., Vol. 28, Page 1217-1227, Year 2014
Publish dateMar 8, 2014 (structure data deposition date)
AuthorsLi, Y. / Zhang, L. / Liu, T. / Chai, C. / Fang, Q. / Wu, H. / Agudelo garcia, P.A. / Han, Z. / Zong, S. / Yu, Y. ...Li, Y. / Zhang, L. / Liu, T. / Chai, C. / Fang, Q. / Wu, H. / Agudelo garcia, P.A. / Han, Z. / Zong, S. / Yu, Y. / Zhang, X. / Parthun, M.R. / Chai, J. / Xu, R.M. / Yang, M.
External linksGenes Dev. / PubMed:24835250
MethodsX-ray diffraction
Resolution2.101 - 2.509 Å
Structure data

PDB-4psw:
Crystal structure of histone acetyltransferase complex
Method: X-RAY DIFFRACTION / Resolution: 2.101 Å

PDB-4psx:
Crystal structure of histone acetyltransferase complex
Method: X-RAY DIFFRACTION / Resolution: 2.509 Å

Chemicals

ChemComp-COA:
COENZYME A

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • ophiophagus hannah (king cobra)
  • saccharomyces cerevisiae s288c (yeast)
KeywordsTRANSFERASE / HAT WD40 / histone acetyltransferase / AcCoA / Phosphorylation / Cytoplasmatic / HISTONE/TRANSFERASE / acetyltransferase / HISTONE-TRANSFERASE complex

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