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Structure paper

TitleContributions of a unique beta-clamp to substrate recognition illuminates the molecular basis of exolysis in ferulic acid esterases.
Journal, issue, pagesBiochem. J., Vol. 473, Page 839-849, Year 2016
Publish dateJul 29, 2015 (structure data deposition date)
AuthorsGruninger, R.J. / Cote, C. / McAllister, T.A. / Abbott, D.W.
External linksBiochem. J. / PubMed:27026397
MethodsX-ray diffraction
Resolution1.55 - 1.6 Å
Structure data

PDB-5cxu:
Structure of the CE1 ferulic acid esterase AmCE1/Fae1A, from the anaerobic fungi Anaeromyces mucronatus in the absence of substrate
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-5cxx:
Structure of a CE1 ferulic acid esterase, AmCE1/Fae1A, from Anaeromyces mucronatus in complex with Ferulic acid
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-FER:
3-(4-HYDROXY-3-METHOXYPHENYL)-2-PROPENOIC ACID

ChemComp-SO4:
SULFATE ION

Source
  • anaeromyces mucronatus (fungus)
KeywordsHYDROLASE / Ferulic acid / esterase / induced fit / alpha/beta hydrolase / anaerobic fungi / alpha/beta-hydrolase

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