@article { ISI:000220334900133,
	title = {Crystal structure of Thermotoga maritima alpha-L-fucosidase - Insights into the catalytic mechanism and the molecular basis for fucosidosis},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {279},
	number = {13},
	year = {2004},
	month = {MAR 26},
	pages = {13119-13128},
	abstract = {Fucosylated glycoconjugates are involved in numerous biological events, and alpha-L-fucosidases, the enzymes responsible for their processing, are therefore of crucial importance. Deficiency in alpha-L-fucosidase activity is associated with fucosidosis, a lysosomal storage disorder characterized by rapid neurodegeneration, resulting in severe mental and motor deterioration. To gain insight into alpha-L-fucosidase function at the molecular level, we have determined the crystal structure of Thermotoga maritima alpha-L-fucosidase. This enzyme assembles as a hexamer and displays a two-domain fold, composed of a catalytic (beta/alpha)(8)-like domain and a C-terminal beta-sandwich domain. The structures of an enzyme-product complex and of a covalent glycosyl-enzyme intermediate, coupled with kinetic and mutagenesis studies, allowed us to identify the catalytic nucleophile, Asp(244), and the Bronsted acid/base, Glu(266). Because T. maritima alpha-L-fucosidase occupies a unique evolutionary position, being far more closely related to the mammalian enzymes than to any other prokaryotic homolog, a structural model of the human enzyme was built to document the structural consequences of the genetic mutations associated with fucosidosis.},
	issn = {0021-9258},
	doi = {10.1074/jbc.M313783200},
	author = {Sulzenbacher, G and Bignon, C and Nishimura, T and Tarling, CA and Withers, SG and Henrissat, B and Bourne, Y}
}
