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Atomic (0.94 Å) resolution structure of an inverting glycosidase in complex with substrate

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.
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Submitted on : Wednesday, February 17, 2021 - 6:41:44 PM
Last modification on : Wednesday, March 24, 2021 - 3:21:30 AM

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Diego Guérin, Marie-Bernard Lascombe, Marcelo Costabel, Hélène Souchon, Victor Lamzin, et al.. Atomic (0.94 Å) resolution structure of an inverting glycosidase in complex with substrate. Journal of Molecular Biology, Elsevier, 2002, 316 (5), pp.1061-1069. ⟨10.1006/jmbi.2001.5404⟩. ⟨pasteur-03144720⟩

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