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Structure paper

TitleS-adenosyl methionine is necessary for inhibition of the methyltransferase G9a by the lysine 9 to methionine mutation on histone H3.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 113, Page 6182-6187, Year 2016
Publish dateApr 21, 2016 (structure data deposition date)
AuthorsJayaram, H. / Hoelper, D. / Jain, S.U. / Cantone, N. / Lundgren, S.M. / Poy, F. / Allis, C.D. / Cummings, R. / Bellon, S. / Lewis, P.W.
External linksProc. Natl. Acad. Sci. USA / PubMed:27185940
MethodsX-ray diffraction
Resolution1.48 - 1.85 Å
Structure data

PDB-5jhn:
Structure of G9a SET-domain with Histone H3K9Ala mutant peptide and bound S-adenosylmethionine
Method: X-RAY DIFFRACTION / Resolution: 1.67 Å

PDB-5jin:
Structure of G9a SET-domain with Histone H3K9M mutant peptide and bound S-adenosylmethionine
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-5jiy:
Structure of G9a SET-domain with Histone H3K9norLeucine mutant peptide and bound S-adenosylmethionine
Method: X-RAY DIFFRACTION / Resolution: 1.48 Å

PDB-5jj0:
Structure of G9a SET-domain with Histone H3K9M peptide and excess SAH
Method: X-RAY DIFFRACTION / Resolution: 1.72 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-SAM:
S-ADENOSYLMETHIONINE

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / SET-domain / Histone methyl transferase / histone peptide

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