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Structure paper

TitleRespective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A
Journal, issue, pagesFebs Lett., Vol. 580, Page 5815-5821, Year 2006
Publish dateJul 6, 2006 (structure data deposition date)
AuthorsBenoit, I. / Asther, M. / Sulzenbacher, G. / Record, E. / Marmuse, L. / Parsiegla, G. / Herpoel-Gimbert, I. / Bignon, C.
External linksFebs Lett. / PubMed:17027758
MethodsX-ray diffraction
Resolution1.55 - 1.7 Å
Structure data

PDB-2hl6:
Structure of homologously expressed Ferrulate esterase of Aspergillus niger in complex with CAPS
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-2ix9:
Respective role of protein folding and glycosylation in the thermal stability of recombinant Feruloyl Esterase A
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-CXS:
3-CYCLOHEXYL-1-PROPYLSULFONIC ACID / pH buffer*YM

ChemComp-HOH:
WATER

Source
  • aspergillus niger (mold)
KeywordsHYDROLASE / Esterase / a/b hydrolase fold / glycosylated / CAPS / XYLAN DEGRADATION / FERULOYL ESTERASE EC 3.1.1.73 / GLYCOPROTEIN / SERINE ESTERASE

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