1PS3
Golgi alpha-mannosidase II in complex with kifunensine
Summary for 1PS3
| Entry DOI | 10.2210/pdb1ps3/pdb |
| Related | 1HTY 1HWW 1HXK |
| Descriptor | Alpha-mannosidase II, 2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (6 entities in total) |
| Functional Keywords | glycosyl hydrolase, mannosidase, n-terminal alpha-beta domain, three helix bundle, 2 c-terminal beta barrels, hydrolase |
| Biological source | Drosophila melanogaster (fruit fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 120230.63 |
| Authors | Shah, N.,Kuntz, D.A.,Rose, D.R. (deposition date: 2003-06-20, release date: 2003-12-16, Last modification date: 2024-10-16) |
| Primary citation | Shah, N.,Kuntz, D.A.,Rose, D.R. Comparison of Kifunensine and 1-Deoxymannojirimycin Binding to Class I and II alpha-Mannosidases Demonstrates Different Saccharide Distortions in Inverting and Retaining Catalytic Mechanisms Biochemistry, 42:13812-13816, 2003 Cited by PubMed Abstract: Mannosidases are key enzymes in the eukaryotic N-glycosylation pathway. These enzymes fall into two broad classes (I and II) and are characteristically different in catalytic mechanism, sequence, and structure. Kifunensine is an alkaloid that is a strong inhibitor against class I alpha-mannosidases but is only a weak inhibitor against class II alpha-mannosidases. In this paper, the 1.80 A resolution crystal structure of kifunensine bound to Drosophila melanogaster Golgi alpha-mannosidase II (dGMII) is presented. Kifunensine adopts a (1,4)B boat conformation in the class II dGMII, which contrasts the (1)C(4) chair conformation seen in class I human endoplasmic reticulum alpha1,2 mannosidase (hERMI, PDB ). The observed conformations are higher in conformational energy than the global minimum (4)C(1) conformation, although the conformation in hERMI is closer to the minimum, as supported by an energy calculation. Differing conformations of 1-deoxymannojirimycin were also observed: a (4)C(1) and (1)C(4) conformation in dGMII and hERMI, respectively. Thus, these two alpha-mannosidase classes distort these inhibitors in distinct manners. This is likely indicative of the binding characteristics of the two different catalytic mechanisms of these enzymes. PubMed: 14636047DOI: 10.1021/bi034742r PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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