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Structure paper

TitleStructure-Function Analyses of a Caffeic Acid O-Methyltransferase from Perennial Ryegrass Reveal the Molecular Basis for Substrate Preference.
Journal, issue, pagesPlant Cell, Vol. 22, Page 4114-4127, Year 2010
Publish dateOct 17, 2010 (structure data deposition date)
AuthorsLouie, G.V. / Bowman, M.E. / Tu, Y. / Mouradov, A. / Spangenberg, G. / Noel, J.P.
External linksPlant Cell / PubMed:21177481
MethodsX-ray diffraction
Resolution1.8 - 2.25 Å
Structure data

PDB-3p9c:
Crystal structure of perennial ryegrass LpOMT1 bound to SAH
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3p9i:
Crystal structure of perennial ryegrass LpOMT1 complexed with S-adenosyl-L-homocysteine and sinapaldehyde
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-3p9k:
Crystal structure of perennial ryegrass LpOMT1 complexed with S-adenosyl-L-homocysteine and coniferaldehyde
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

Chemicals

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-DTV:
(2S,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL

ChemComp-ACT:
ACETATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-SNY:
(2E)-3-(4-hydroxy-3,5-dimethoxyphenyl)prop-2-enal

ChemComp-BME:
BETA-MERCAPTOETHANOL

ChemComp-CIY:
(2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enal

Source
  • lolium perenne (perennial ryegrass)
KeywordsTRANSFERASE / S-adenosylmethionine dependent O-methyltransferase

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