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© Institut Pasteur
Cells infected for 24 hrs with C. Trachomatis. The cell nuclei are labelled in blue, the bacteria appear yellow, within the inclusion lumen. A bacterial protein secreted out the inclusion into the host cytoplasm id labelled in red.
Publication : Journal of molecular biology

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of molecular biology - 01 Mar 2002

Guérin DM, Lascombe MB, Costabel M, Souchon H, Lamzin V, Béguin P, Alzari PM

Link to Pubmed [PMID] – 11884144

J. Mol. Biol. 2002 Mar;316(5):1061-9

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.