Structural basis for two-step glucose trimming by glucosidase II involved in ER glycoprotein quality control

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Abstract

The endoplasmic reticulum (ER) has a sophisticated protein quality control system for the efficient folding of newly synthesized proteins. In this system, a variety of N-linked oligosaccharides displayed on proteins serve as signals recognized by series of intracellular lectins. Glucosidase II catalyzes two-step hydrolysis at α1,3-linked glucose-glucose and glucose-mannose residues of high-mannose-type glycans to generate a quality control protein tag that is transiently expressed on glycoproteins and recognized by ER chaperones. Here we determined the crystal structures of the catalytic α subunit of glucosidase II (GIIα) complexed with two different glucosyl ligands containing the scissile bonds of first-and second-step reactions. Our structural data revealed that the nonreducing terminal disaccharide moieties of the two kinds of substrates can be accommodated in a gourd-shaped bilocular pocket, thereby providing a structural basis for substrate-binding specificity in the two-step deglucosylation catalyzed by this enzyme.

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Satoh, T., Toshimori, T., Yan, G., Yamaguchi, T., & Kato, K. (2016). Structural basis for two-step glucose trimming by glucosidase II involved in ER glycoprotein quality control. Scientific Reports, 6. https://doi.org/10.1038/srep20575

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