6FOA
Human Xylosyltransferase 1 apo structure
Summary for 6FOA
| Entry DOI | 10.2210/pdb6foa/pdb |
| Descriptor | Xylosyltransferase 1, 2-acetamido-2-deoxy-beta-D-glucopyranose, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | proteoglycan, glycosyltransferase, golgi, xylosyltransferase, transferase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 86461.22 |
| Authors | Briggs, D.C.,Hohenester, E. (deposition date: 2018-02-06, release date: 2018-05-02, Last modification date: 2024-11-13) |
| Primary citation | Briggs, D.C.,Hohenester, E. Structural Basis for the Initiation of Glycosaminoglycan Biosynthesis by Human Xylosyltransferase 1. Structure, 26:801-809.e3, 2018 Cited by PubMed Abstract: 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. PubMed: 29681470DOI: 10.1016/j.str.2018.03.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.869 Å) |
Structure validation
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