5dl0

Crystal structure of glucosidase II alpha subunit (Glc1Man2-bound from)

spinqualitylabelsall models 5dl0, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5dl0 is a 1 chain structure with sequence from Chaetomium thermophilum var. thermophilum DSM 1495. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: GLC, MAN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G0SG42_CHATD Publication Abstract from PubMed 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 alpha1,3-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 alpha subunit of glucosidase II (GIIalpha) 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. Structural basis for two-step glucose trimming by glucosidase II involved in ER glycoprotein quality control.,Satoh T, Toshimori T, Yan G, Yamaguchi T, Kato K Sci Rep. 2016 Feb 5;6:20575. doi: 10.1038/srep20575. PMID:26847925 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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