@article { ISI:000079918200020,
	title = {The crystal structure of a 2-fluorocellotriosyl complex of the Streptomyces lividans endoglucanase CelB2 at 1.2 angstrom resolution},
	journal = {BIOCHEMISTRY},
	volume = {38},
	number = {15},
	year = {1999},
	month = {APR 13},
	pages = {4826-4833},
	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 {\textquoteleft}{\textquoteleft}clans{{\textquoteright}{\textquoteright}} 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 beta-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 Angstrom) data allow clear identification of two distinct species in the crystal. One is the glycosyl-enzyme 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-beta-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.},
	issn = {0006-2960},
	doi = {10.1021/bi982648i},
	author = {Sulzenbacher, G and MacKenzie, LF and Wilson, KS and Withers, SG and Dupont, C and Davies, GJ}
}
