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TitleCatalysis and Specificity in Enzymatic Glycoside Hydrolysis: A 2,5B Conformation for the Glycosyl-Enzyme Intermediate Revealed by the Structure of the Bacillus Agaradhaerens Family 11 Xylanase.
Journal, issue, pagesChem. Biol., Vol. 6, Page 483-, Year 1999
Publish dateMay 11, 2001 (structure data deposition date)
AuthorsSabini, E. / Sulzenbacher, G. / Dauter, M. / Dauter, Z. / Jorgensen, P.L. / Schulein, M. / Dupont, C. / Davies, G.J. / Wilson, K.S.
External linksChem. Biol. / PubMed:10381409
MethodsX-ray diffraction
Resolution1.1 - 2 Å
Structure data

PDB-1h4g:
Oligosaccharide-binding to family 11 xylanases: both covalent intermediate and mutant-product complexes display 2,5B conformations at the active-centre
Method: X-RAY DIFFRACTION / Resolution: 1.1 Å

PDB-1h4h:
Oligosaccharide-binding to family 11 xylanases: both covalent intermediate and mutant-product complexes display 2,5B conformations at the active-centre
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1qh6:
CATALYSIS AND SPECIFICITY IN ENZYMATIC GLYCOSIDE HYDROLASES: A 2,5B CONFORMATION FOR THE GLYCOSYL-ENZYME INTERMIDIATE REVEALED BY THE STRUCTURE OF THE BACILLUS AGARADHAERENS FAMILY 11 XYLANASE
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1qh7:
CATALYSIS AND SPECIFICITY IN ENZYMATIC GLYCOSIDE HYDROLASES: A 2,5B CONFORMATION FOR THE GLYCOSYL-ENZYME INTERMIDIATE REVEALED BY THE STRUCTURE OF THE BACILLUS AGARADHAERENS FAMILY 11 XYLANASE
Method: X-RAY DIFFRACTION / Resolution: 1.78 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-XYP:
beta-D-xylopyranose

Source
  • bacillus agaradhaerens (bacteria)
KeywordsGLYCOSIDE HYDROLASE / XYLANASE / OLIGOSACCHARIDE / TRANSITION-STATE / INTERMEDIATE / MUTANT / BOAT CONFORMATION / HYDROLASE / GLYCOSYL HYDROLASE

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