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Crystal structure of a class I α1,2‐mannosidase involved in N ‐glycan processing and endoplasmic reticulum quality control
Author(s) -
Vallée François,
Lipari Francesco,
Yip Patrick,
Sleno Barry,
Herscovics Annette,
Howell P.Lynne
Publication year - 2000
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/19.4.581
Subject(s) - endoplasmic reticulum , biology , mannosidase , glycan , stim1 , crystal (programming language) , microbiology and biotechnology , biochemistry , enzyme , glycoprotein , computer science , programming language
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 α1,2‐mannosidase that trims Man 9 GlcNAc 2 to Man 8 GlcNAc 2 isomer B in the endoplasmic reticulum of Saccharomyces cerevisiae reveals a novel (αα) 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.