9sd6

Crystal structure of the C-terminally truncated human E430Q/E574Q-PGGHG double mutant in complex with kojibiose

spinqualitylabelsall models 9sd6, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9sd6 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: BGC, CL, GLC, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PGGHG_HUMAN Catalyzes the hydrolysis of glucose from the disaccharide unit linked to hydroxylysine residues of collagen and collagen-like proteins. Publication Abstract from PubMed The enzyme glucosylgalactosylhydroxylysine glucosidase (PGGHG) plays a critical role in collagen metabolism by hydrolyzing the 2-O-alpha-d-glucopyranosyl-O-beta-d-galactopyranose, a natural disaccharide found in the glycosylation of hydroxylysine residues in collagen. We report the X-ray crystallographic structure of human PGGHG, revealing the canonical four-domain fold of enzymes from the GH65 family and representing the first structure reported for a mammalian enzyme in this family. A distinctive flat surface adjacent to the catalytic site, shaped by the N-terminal beta-sheet and specific conformations of catalytic loops, is unique to PGGHG among GH65 enzymes. Structural complexes with glucose and the substrate analogue kojibiose (KJB), along with site-directed mutagenesis and enzyme assays, identify residues critical for catalysis and hydroxylysine-collagen binding. Docking studies and AlphaFold3-based predictions suggest that the flat surface facilitates the contact between PGGHG and collagen peptides as well as substrate recognition, and support the enzyme's high specificity toward its glucosaccharide substrate. These findings provide structural insight into the selective recognition of glycosylated hydroxylysines and may inform future therapeutic or biotechnological applications targeting collagen metabolism. The structure of human glucosidase PGGHG reveals a very specific active site accessible through a flat surface for collagen approximation.,Casas-Florez D, Ortega-Garcia R, Sanz-Benito P, Monterroso B, Sanz-Aparicio J, Gonzalez B Int J Biol Macromol. 2026 Feb;345:150556. doi: 10.1016/j.ijbiomac.2026.150556. , Epub 2026 Jan 26. PMID:41605404 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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