1H4H

Oligosaccharide-binding to family 11 xylanases: both covalent intermediate and mutant-product complexes display 2,5B conformations at the active-centre

Summary for 1H4H

• Entry DOI: 10.2210/pdb1h4h/pdb
• Related: 1H4G
• Descriptor: XYLANASE, beta-D-xylopyranose-(1-4)-beta-D-xylopyranose-(1-4)-alpha-D-xylopyranose (3 entities in total)
• Functional Keywords: glycoside hydrolase, xylanase, oligosaccharide, transition-state, intermediate, mutant, boat conformation
• Biological source: BACILLUS AGARADHAERENS
• Total number of polymer chains: 4
• Total formula weight: 94904.53

Authors

Sabini, E.,Wilson, K.S.,Danielsen, S.,Schulein, M.,Davies, G.J. (deposition date: 2001-05-11, release date: 2002-05-09, Last modification date: 2024-11-06)

Primary citation

Sabini, E.,Sulzenbacher, G.,Dauter, M.,Dauter, Z.,Jorgensen, P.L.,Schulein, M.,Dupont, C.,Davies, G.J.,Wilson, K.S.
Catalysis 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.
Chem.Biol., 6:483-, 1999

PubMed Abstract: The enzymatic hydrolysis of glycosides involves the formation and subsequent breakdown of a covalent glycosyl-enzyme intermediate via oxocarbenium-ion-like transition states. The covalent intermediate may be trapped on-enzyme using 2-fluoro-substituted glycosides, which provide details of the intermediate conformation and noncovalent interactions between enzyme and oligosaccharide. Xylanases are important in industrial applications - in the pulp and paper industry, pretreating wood with xylanases decreases the amount of chlorine-containing chemicals used. Xylanases are structurally similar to cellulases but differ in their specificity for xylose-based, versus glucose-based, substrates.

PubMed: 10381409
DOI: 10.1016/S1074-5521(99)80066-0

Experimental method

X-RAY DIFFRACTION (1.9 Å)