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

Authors
Guérin, Diego Marcelo Alejandro; Lascombe, Marie-Bernard; Costabel, Marcelo Daniel; Souchon, Hélène; Lamzin, Victor; Béguin, Pierre; Alzari, Pedro M
Publication Year
2002
Language
English
Format
article
Status
Published version
Description
The crystal structure of Clostridium thermocellum endoglucanase CelA in complex with cellopentaose has been determined at 0.94 Å 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 boat2,5 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. © 2002 Elsevier Science Ltd.
Fil: Guérin, Diego Marcelo Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Pasteur; Francia. Hamburg Outstation; Alemania
Fil: Lascombe, Marie-Bernard. Instituto Pasteur; Francia
Fil: Costabel, Marcelo Daniel. Instituto Pasteur; Francia. Hamburg Outstation; Alemania
Fil: Souchon, Hélène. Instituto Pasteur; Francia
Fil: Lamzin, Victor. Hamburg Outstation; Alemania
Fil: Béguin, Pierre. Instituto Pasteur; Francia
Fil: Alzari, Pedro M. Instituto Pasteur; Francia
Subject
ATOMIC RESOLUTION
INVERTING GLYCOSIDASE
PROTEIN-CARBOHYDRATE INTERACTIONS
REACTION MECHANISM
X-RAY CRYSTALLOGRAPHY
Otras Ciencias Biológicas
Ciencias Biológicas
CIENCIAS NATURALES Y EXACTAS
Access level
Open access
License
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repository
CONICET Digital (CONICET)
Institution
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identifier
oai:ri.conicet.gov.ar:11336/71438