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TitleThe double PHD finger domain of MOZ/MYST3 induces alpha-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification.
Journal, issue, pagesNucleic Acids Res., Vol. 42, Page 822-835, Year 2014
Publish dateJul 5, 2013 (structure data deposition date)
AuthorsDreveny, I. / Deeves, S.E. / Fulton, J. / Yue, B. / Messmer, M. / Bhattacharya, A. / Collins, H.M. / Heery, D.M.
External linksNucleic Acids Res. / PubMed:24150941
MethodsX-ray diffraction
Resolution1.6 - 3 Å
Structure data

PDB-4ljn:
Crystal Structure of MOZ double PHD finger
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-4lk9:
Crystal Structure of MOZ double PHD finger histone H3 tail complex
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-4lka:
Crystal Structure of MOZ double PHD finger histone H3K9ac complex
Method: X-RAY DIFFRACTION / Resolution: 1.61 Å

PDB-4llb:
Crystal Structure of MOZ double PHD finger histone H3K14ac complex
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / plant homeodomain finger / double PHD / Zinc Finger / histone acetyl transferase / double PHD finger / DPF / histone acetyltransferase / histone H3 / H3 tail / histone H3 tail acetylated at K9 / DPF - H3K14ac complex / plant homeodomain / histone H3 tail

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