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TitleEngineering Hyperthermostability Into a Gh11 Xylanase is Mediated by Subtle Changes to Protein Structure.
Journal, issue, pagesJ. Biol. Chem., Vol. 283, Page 22557-, Year 2008
Publish dateMay 26, 2008 (structure data deposition date)
AuthorsDumon, C. / Varvak, A. / Wall, M.A. / Flint, J.E. / Lewis, R.J. / Lakey, J.H. / Morland, C. / Luginbuhl, P. / Healey, S. / Todaro, T. ...Dumon, C. / Varvak, A. / Wall, M.A. / Flint, J.E. / Lewis, R.J. / Lakey, J.H. / Morland, C. / Luginbuhl, P. / Healey, S. / Todaro, T. / Desantis, G. / Sun, M. / Parra-Gessert, L. / Tan, X. / Weiner, D.P. / Gilbert, H.J.
External linksJ. Biol. Chem. / PubMed:18515360
MethodsX-ray diffraction
Resolution1.8 - 1.9 Å
Structure data

PDB-2vuj:
Environmentally isolated GH11 xylanase
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2vul:
Thermostable mutant of ENVIRONMENTALLY ISOLATED GH11 XYLANASE
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-12P:
DODECAETHYLENE GLYCOL / precipitant*YM

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / GH11 / XYLANASE / GLYCOSIDASE

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