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TitleConformational changes in the di-domain structure of Arabidopsis phosphoethanolamine methyltransferase leads to active-site formation.
Journal, issue, pagesJ. Biol. Chem., Vol. 292, Page 21690-21702, Year 2017
Publish dateAug 3, 2017 (structure data deposition date)
AuthorsLee, S.G. / Jez, J.M.
External linksJ. Biol. Chem. / PubMed:29084845
MethodsX-ray diffraction
Resolution1.341 - 1.5 Å
Structure data

PDB-5wp4:
Arabidopsis thaliana phosphoethanolamine N-methyltransferase 1 (AtPMT1, XIOPTL) in complex with SAH and phosphocholine
Method: X-RAY DIFFRACTION / Resolution: 1.341 Å

PDB-5wp5:
Arabidopsis thaliana phosphoethanolamine N-methyltransferase 2 (AtPMT2) in complex with SAH
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-PC:
PHOSPHOCHOLINE

ChemComp-HOH:
WATER

Source
  • arabidopsis thaliana (thale cress)
KeywordsTRANSFERASE / Phosphoethanolamine N-Methyltransferase / AtPMT1 / XIOPTL / AtPMT2

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