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Structure paper

TitleEvolution of structure and mechanistic divergence in di-domain methyltransferases from nematode phosphocholine biosynthesis.
Journal, issue, pagesStructure, Vol. 21, Page 1778-1787, Year 2013
Publish dateMay 16, 2013 (structure data deposition date)
AuthorsLee, S.G. / Jez, J.M.
External linksStructure / PubMed:24012478
MethodsX-ray diffraction
Resolution1.68 - 3 Å
Structure data

PDB-4krg:
SeMet Haemonchus contortus Phosphoethanolamine N-methyltransferase 1 in complex with phosphoethanolamine and S-adenosylhomocysteine
Method: X-RAY DIFFRACTION / Resolution: 1.68 Å

PDB-4krh:
SeMet Haemonchus contortus Phosphoethanolamine N-methyltransferase 2 in complex with S-adenosyl-L-methionine
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-4kri:
Haemonchus contortus Phospholethanolamine N-methyltransferase 2 in complex with phosphomonomethylethanolamine and S-adenosylhomocysteine
Method: X-RAY DIFFRACTION / Resolution: 1.72 Å

Chemicals

ChemComp-OPE:
PHOSPHORIC ACID MONO-(2-AMINO-ETHYL) ESTER

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-BOG:
octyl beta-D-glucopyranoside / detergent*YM

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SAM:
S-ADENOSYLMETHIONINE

ChemComp-1SH:
2-(methylamino)ethyl dihydrogen phosphate

Source
  • haemonchus contortus (barber pole worm)
KeywordsTRANSFERASE / methyltransferase / phosphoethanolamine / S-adenosylmethionine

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