1qx1
Golgi alpha-mannosidase II D341N mutant complex with 2-F-mannosyl-F
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OverviewOverview
The family 38 golgi alpha-mannosidase II, thought to cleave mannosidic, bonds through a double displacement mechanism involving a reaction, intermediate, is a clinically important enzyme involved in glycoprotein, processing. The structure of three different covalent glycosyl-enzyme, intermediates have been determined to 1.2-A resolution for the Golgi, alpha-mannosidase II from Drosophila melanogaster by use of fluorinated, sugar analogues, both with the wild-type enzyme and a mutant enzyme in, which the acid/base catalyst has been removed. All these structures reveal, sugar intermediates bound in a distorted 1S5 skew boat conformation. The, similarity of this conformation with that of the substrate in the recently, determined structure of the Michaelis complex of a beta-mannanase (Ducros, V. M. A., Zechel, D. L., Murshudov, G. N., Gilbert, H. J., Szabo, L., Stoll, D., Withers, S. G., and Davies, G. J. (2002) Angew. Chem. Int. Ed., Engl. 41, 2824-2827) suggests that these disparate enzymes have recruited, common stereoelectronic features in evolving their catalytic mechanisms.
About this StructureAbout this Structure
1QX1 is a Single protein structure of sequence from Drosophila melanogaster with NAG, ZN, FMF and MPD as ligands. Active as Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase, with EC number 3.2.1.114 Full crystallographic information is available from OCA.
ReferenceReference
Insights into the mechanism of Drosophila melanogaster Golgi alpha-mannosidase II through the structural analysis of covalent reaction intermediates., Numao S, Kuntz DA, Withers SG, Rose DR, J Biol Chem. 2003 Nov 28;278(48):48074-83. Epub 2003 Sep 5. PMID:12960159
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