1QX1
Golgi alpha-mannosidase II D341N mutant complex with 2-F-mannosyl-F
Summary for 1QX1
| Entry DOI | 10.2210/pdb1qx1/pdb |
| Related | 1HTY 1HWW 1HXK 1PS3 1QWN 1QWU |
| Descriptor | Alpha-mannosidase II, 2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (6 entities in total) |
| Functional Keywords | glycosyl hydrolase family 38, covalent catalytic intermediate, hydrolase |
| Biological source | Drosophila melanogaster (fruit fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 120289.56 |
| Authors | Numao, S.,Kuntz, D.A.,Withers, S.G.,Rose, D.R. (deposition date: 2003-09-04, release date: 2003-10-07, Last modification date: 2024-10-30) |
| Primary citation | Numao, S.,Kuntz, D.A.,Withers, S.G.,Rose, D.R. Insights into the mechanism of Drosophila melanogaster Golgi alpha-mannosidase II through the structural analysis of covalent reaction intermediates. J.Biol.Chem., 278:48074-48083, 2003 Cited by PubMed Abstract: 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. PubMed: 12960159DOI: 10.1074/jbc.M309249200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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