1DL2
CRYSTAL STRUCTURE OF CLASS I ALPHA-1,2-MANNOSIDASE FROM SACCHAROMYCES CEREVISIAE AT 1.54 ANGSTROM RESOLUTION
Summary for 1DL2
| Entry DOI | 10.2210/pdb1dl2/pdb |
| Descriptor | CLASS I ALPHA-1,2-MANNOSIDASE, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | alpha-alpha helix barrel, hydrolase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Total number of polymer chains | 1 |
| Total formula weight | 60948.04 |
| Authors | Vallee, F.,Lipari, F.,Yip, P.,Herscovics, A.,Howell, P.L. (deposition date: 1999-12-08, release date: 2000-02-18, Last modification date: 2024-11-13) |
| Primary citation | Vallee, F.,Lipari, F.,Yip, P.,Sleno, B.,Herscovics, A.,Howell, P.L. Crystal structure of a class I alpha1,2-mannosidase involved in N-glycan processing and endoplasmic reticulum quality control. EMBO J., 19:581-588, 2000 Cited by PubMed Abstract: Mannose trimming is not only essential for N-glycan maturation in mammalian cells but also triggers degradation of misfolded glycoproteins. The crystal structure of the class I alpha1, 2-mannosidase that trims Man(9)GlcNAc(2) to Man(8)GlcNAc(2 )isomer B in the endoplasmic reticulum of Saccharomyces cerevisiae reveals a novel (alphaalpha)(7)-barrel in which an N-glycan from one molecule extends into the barrel of an adjacent molecule, interacting with the essential acidic residues and calcium ion. The observed protein-carbohydrate interactions provide the first insight into the catalytic mechanism and specificity of this eukaryotic enzyme family and may be used to design inhibitors that prevent degradation of misfolded glycoproteins in genetic diseases. PubMed: 10675327DOI: 10.1093/emboj/19.4.581 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.54 Å) |
Structure validation
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