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Structure paper

TitleCatalytic Roles for Carbon-Oxygen Hydrogen Bonding in SET Domain Lysine Methyltransferases.
Journal, issue, pagesJ. Biol. Chem., Vol. 281, Page 19280-19287, Year 2006
Publish dateMay 17, 2006 (structure data deposition date)
AuthorsCouture, J.F. / Hauk, G. / Thompson, M.J. / Blackburn, G.M. / Trievel, R.C.
External linksJ. Biol. Chem. / PubMed:16682405
MethodsX-ray diffraction
Resolution2.45 - 2.6 Å
Structure data

PDB-2h21:
Structure of Rubisco LSMT bound to AdoMet
Method: X-RAY DIFFRACTION / Resolution: 2.45 Å

PDB-2h23:
Structure of Rubisco LSMT bound to Trimethyllysine and AdoHcy
Method: X-RAY DIFFRACTION / Resolution: 2.45 Å

PDB-2h2e:
Structure of Rubisco LSMT bound to AzaAdoMet and Lysine
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-2h2j:
Structure of Rubisco LSMT bound to Sinefungin and Monomethyllysine
Method: X-RAY DIFFRACTION / Resolution: 2.45 Å

Chemicals

ChemComp-SAM:
S-ADENOSYLMETHIONINE

ChemComp-HOH:
WATER

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-M3L:
N-TRIMETHYLLYSINE

ChemComp-SA8:
S-5'-AZAMETHIONINE-5'-DEOXYADENOSINE

ChemComp-LYS:
LYSINE

ChemComp-SFG:
SINEFUNGIN

ChemComp-MLZ:
N-METHYL-LYSINE

Source
  • pisum sativum (garden pea)
KeywordsTRANSFERASE / SET domain / protein lysine methyltransferase

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