1KWF

Atomic Resolution Structure of an Inverting Glycosidase in Complex with Substrate

Summary for 1KWF

• Entry DOI: 10.2210/pdb1kwf/pdb
• Related: 1CEM
• Related PRD ID: PRD_900016
• Descriptor: Endoglucanase A, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: hydrolase, inverting glycosidase, atomic resolution, protein-carbohydrate interactions, reaction mechanism, cellulase
• Biological source: Clostridium thermocellum
• Total number of polymer chains: 1
• Total formula weight: 41698.51

Authors

Guerin, D.M.A.,Lascombe, M.-B.,Costabel, M.,Souchon, H.,Lamzin, V.,Beguin, P.,Alzari, P.M. (deposition date: 2002-01-29, release date: 2002-03-13, Last modification date: 2024-02-14)

Primary citation

Guerin, D.M.,Lascombe, M.B.,Costabel, M.,Souchon, H.,Lamzin, V.,Beguin, P.,Alzari, P.M.
Atomic (0.94 A) resolution structure of an inverting glycosidase in complex with substrate.
J.Mol.Biol., 316:1061-1069, 2002

PubMed Abstract: The crystal structure of Clostridium thermocellum endoglucanase CelA in complex with cellopentaose has been determined at 0.94 A resolution. The oligosaccharide occupies six D-glucosyl-binding subsites, three on either side of the scissile glycosidic linkage. The substrate and product of the reaction occupy different positions at the reducing end of the cleft, where an extended array of hydrogen-bonding interactions with water molecules fosters the departure of the leaving group. Severe torsional strain upon the bound substrate forces a distorted boat(2,5) B conformation for the glucosyl residue bound at subsite -1, which facilitates the formation of an oxocarbenium ion intermediate and might favor the breakage of the sugar ring concomitant with catalysis.

PubMed: 11884144
DOI: 10.1006/jmbi.2001.5404

Experimental method

X-RAY DIFFRACTION (0.94 Å)