The Crystal Structure of a 2-Fluorocellotriosyl Complex of the Streptomyces lividans Endoglucanase CelB2 at 1.2 Å Resolution † , ‡ - Archive ouverte HAL Access content directly
Journal Articles Biochemistry Year : 1999

The Crystal Structure of a 2-Fluorocellotriosyl Complex of the Streptomyces lividans Endoglucanase CelB2 at 1.2 Å Resolution † , ‡

Abstract

Glycoside hydrolases have been classified into over 66 families on the basis of amino acid sequence. Recently a number of these families have been grouped into "clans" which share a common fold and catalytic mechanism [Henrissat, B., and Bairoch, A. (1996) Biochem. J. 316, 695-696]. Glycoside hydrolase Clan GH-C groups family 11 xylanases and family 12 cellulases, which share the same jellyroll topology, with two predominantly antiparallel-sheets forming a long substrate-binding cleft, and act with net retention of anomeric configuration. Here we present the three-dimensional structure of a family 12 endoglucanase, Streptomyces liVidans CelB2, in complex with a 2-deoxy-2-fluorocellotrioside. Atomic resolution (1.2 Å) data allow clear identification of two distinct species in the crystal. One is the glycosylenzyme intermediate, with the mechanism-based inhibitor covalently linked to the nucleophile Glu 120, and the other a complex with the reaction product, 2-deoxy-2-fluoro-D-cellotriose. The active site architecture of the complex provides insight into the double-displacement mechanism of retaining glycoside hydrolases and also sheds light on the basis of the differences in specificity between family 12 cellulases and family 11 xylanases.

Dates and versions

hal-03160717 , version 1 (05-03-2021)

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Gerlind Sulzenbacher, Lloyd F Mackenzie, Keith S Wilson, Stephen G Withers, Claude Dupont, et al.. The Crystal Structure of a 2-Fluorocellotriosyl Complex of the Streptomyces lividans Endoglucanase CelB2 at 1.2 Å Resolution † , ‡. Biochemistry, 1999, 38 (15), pp.4826-4833. ⟨10.1021/bi982648i⟩. ⟨hal-03160717⟩
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