Structural highlights
Function
[GUNA_CLOTM] This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Atomic (0.94 A) resolution structure of an inverting glycosidase in complex with substrate.,Guerin DM, Lascombe MB, Costabel M, Souchon H, Lamzin V, Beguin P, Alzari PM J Mol Biol. 2002 Mar 8;316(5):1061-9. PMID:11884144[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Guerin DM, Lascombe MB, Costabel M, Souchon H, Lamzin V, Beguin P, Alzari PM. Atomic (0.94 A) resolution structure of an inverting glycosidase in complex with substrate. J Mol Biol. 2002 Mar 8;316(5):1061-9. PMID:11884144 doi:10.1006/jmbi.2001.5404
