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Structure paper

TitleKMT9 monomethylates histone H4 lysine 12 and controls proliferation of prostate cancer cells.
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 26, Page 361-371, Year 2019
Publish dateJul 11, 2018 (structure data deposition date)
AuthorsMetzger, E. / Wang, S. / Urban, S. / Willmann, D. / Schmidt, A. / Offermann, A. / Allen, A. / Sum, M. / Obier, N. / Cottard, F. ...Metzger, E. / Wang, S. / Urban, S. / Willmann, D. / Schmidt, A. / Offermann, A. / Allen, A. / Sum, M. / Obier, N. / Cottard, F. / Ulferts, S. / Preca, B.T. / Hermann, B. / Maurer, J. / Greschik, H. / Hornung, V. / Einsle, O. / Perner, S. / Imhof, A. / Jung, M. / Schule, R.
External linksNat. Struct. Mol. Biol. / PubMed:31061526
MethodsX-ray diffraction
Resolution1.9 - 1.94 Å
Structure data

PDB-6h1d:
Crystal structure of C21orf127-TRMT112 in complex with SAH
Method: X-RAY DIFFRACTION / Resolution: 1.94 Å

PDB-6h1e:
Crystal structure of C21orf127-TRMT112 in complex with SAH and H4 peptide
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsGENE REGULATION / protein methyltransferase / histone methylation / complex / SAH

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