6ejd

Human Xylosyltransferase 1 in complex with peptide QEEEGSGGPQGG

spinqualitylabelsall models 6ejd, resolution 2.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ejd is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PO4 Activity: Protein xylosyltransferase, with EC number 2.4.2.26 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease [XYLT1_HUMAN] XYLT1-CDG;Desbuquois syndrome. The disease is caused by mutations affecting the gene represented in this entry. The gene represented in this entry acts as a disease modifier. Function [XYLT1_HUMAN] Catalyzes the first step in biosynthesis of glycosaminoglycan. Transfers D-xylose from UDP-D-xylose to specific serine residues of the core protein. Initial enzyme in the biosynthesis of chondroitin sulfate and dermatan sulfate proteoglycans in fibroblasts and chondrocytes. [AMBP_HUMAN] Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization. Trypstatin is a trypsin inhibitor (By similarity). Publication Abstract from PubMed Proteoglycans (PGs) are essential components of the animal extracellular matrix and are required for cell adhesion, migration, signaling, and immune function. PGs are composed of a core protein and long glycosaminoglycan (GAG) chains, which often specify PG function. GAG biosynthesis is initiated by peptide O-xylosyltransferases, which transfer xylose onto selected serine residues in the core proteins. We have determined crystal structures of human xylosyltransferase 1 (XT1) in complex with the sugar donor, UDP-xylose, and various acceptor peptides. The structures reveal unique active-site features that, in conjunction with functional experiments, explain the substrate specificity of XT1. A constriction within the peptide binding cleft requires the acceptor serine to be followed by glycine or alanine. The remainder of the cleft can accommodate a wide variety of sequences, but with a general preference for acidic residues. These findings provide a framework for understanding the selectivity of GAG attachment. Structural Basis for the Initiation of Glycosaminoglycan Biosynthesis by Human Xylosyltransferase 1.,Briggs DC, Hohenester E Structure. 2018 Apr 10. pii: S0969-2126(18)30095-9. doi:, 10.1016/j.str.2018.03.014. PMID:29681470 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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