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Structure paper

TitleStructure of the arginine methyltransferase PRMT5-MEP50 reveals a mechanism for substrate specificity
Journal, issue, pagesPlos One, Vol. 8, Page e57008-e57008, Year 2013
Publish dateJul 17, 2012 (structure data deposition date)
AuthorsHo, M.C. / Wilczek, C. / Bonanno, J.B. / Xing, L. / Seznec, J. / Matsui, T. / Carter, L.G. / Onikubo, T. / Kumar, P.R. / Chan, M.K. ...Ho, M.C. / Wilczek, C. / Bonanno, J.B. / Xing, L. / Seznec, J. / Matsui, T. / Carter, L.G. / Onikubo, T. / Kumar, P.R. / Chan, M.K. / Brenowitz, M. / Cheng, R.H. / Reimer, U. / Almo, S.C. / Shechter, D.
External linksPlos One / PubMed:23451136
MethodsX-ray diffraction
Resolution2.95 Å
Structure data

PDB-4g56:
Crystal Structure of full length PRMT5/MEP50 complexes from Xenopus laevis
Method: X-RAY DIFFRACTION / Resolution: 2.95 Å

Chemicals

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-HOH:
WATER

Source
  • xenopus laevis (African clawed frog)
KeywordsTRANSFERASE / protein arginine methyltransferase / protein complexes / histone methylation / Structural Genomics / PSI-Biology / New York Structural Genomics Research Consortium / NYSGRC

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