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TitleMechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT
Journal, issue, pagesNat. Struct. Biol., Vol. 10, Page 545-552, Year 2003
Publish dateApr 9, 2003 (structure data deposition date)
AuthorsTrievel, R.C. / Flynn, E.M. / Houtz, R.L. / Hurley, J.H.
External linksNat. Struct. Biol. / PubMed:12819771
MethodsX-ray diffraction
Resolution2.55 - 2.65 Å
Structure data

PDB-1ozv:
Crystal structure of the SET domain of LSMT bound to Lysine and AdoHcy
Method: X-RAY DIFFRACTION / Resolution: 2.65 Å

PDB-1p0y:
Crystal structure of the SET domain of LSMT bound to MeLysine and AdoHcy
Method: X-RAY DIFFRACTION / Resolution: 2.55 Å

Chemicals

ChemComp-LYS:
LYSINE

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-HOH:
WATER

ChemComp-MLZ:
N-METHYL-LYSINE

Source
  • pisum sativum (garden pea)
KeywordsTRANSFERASE / SET DOMAIN / LYSINE N-METHYLATION / MULTIPLE METHYLATION / PHOTOSYNTHESIS / POST-TRANSLATIONAL MODIFICATION

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