6h0b | pdb_00006h0b

Crystal structure of the human GalNAc-T4 in complex with UDP, manganese and the diglycopeptide 6.

spinqualitylabelsall models 6h0b, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6h0b is a 3 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 1.8Å Ligands: EDO, GOL, MN, NGA, UDP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GALT4_HUMAN Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a highest activity toward Muc7, EA2 and Muc2, with a lowest activity than GALNT2. Glycosylates 'Thr-57' of SELPLG. Publication Abstract from PubMed Mucin-type O-glycosylation is initiated by a family of polypeptide GalNAc-transferases (GalNAc-Ts) which are type-II transmembrane proteins that contain Golgi luminal catalytic and lectin domains that are connected by a flexible linker. Several GalNAc-Ts, including GalNAc-T4, show both long-range and short-range prior glycosylation specificity, governed by their lectin and catalytic domains, respectively. While the mechanism of the lectin-domain-dependent glycosylation is well-known, the molecular basis for the catalytic-domain-dependent glycosylation of glycopeptides is unclear. Herein, we report the crystal structure of GalNAc-T4 bound to the diglycopeptide GAT*GAGAGAGT*TPGPG (containing two alpha-GalNAc glycosylated Thr (T*), the PXP motif and a "naked" Thr acceptor site) that describes its catalytic domain glycopeptide GalNAc binding site. Kinetic studies of wild-type and GalNAc binding site mutant enzymes show the lectin domain GalNAc binding activity dominates over the catalytic domain GalNAc binding activity and that these activities can be independently eliminated. Surprisingly, a flexible loop protruding from the lectin domain was found essential for the optimal activity of the catalytic domain. This work provides the first structural basis for the short-range glycosylation preferences of a GalNAc-T. Structural and Mechanistic Insights into the Catalytic-Domain-Mediated Short-Range Glycosylation Preferences of GalNAc-T4.,de Las Rivas M, Paul Daniel EJ, Coelho H, Lira-Navarrete E, Raich L, Companon I, Diniz A, Lagartera L, Jimenez-Barbero J, Clausen H, Rovira C, Marcelo F, Corzana F, Gerken TA, Hurtado-Guerrero R ACS Cent Sci. 2018 Sep 26;4(9):1274-1290. doi: 10.1021/acscentsci.8b00488. Epub, 2018 Sep 14. PMID:30276263 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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