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| | ==Human Xylosyltransferase 1 in complex with peptide QEEEGSGVGQGG== | | ==Human Xylosyltransferase 1 in complex with peptide QEEEGSGVGQGG== |
| - | <StructureSection load='6ejc' size='340' side='right' caption='[[6ejc]], [[Resolution|resolution]] 2.06Å' scene=''> | + | <StructureSection load='6ejc' size='340' side='right'caption='[[6ejc]], [[Resolution|resolution]] 2.06Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ejc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EJC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EJC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ejc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EJC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EJC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.057Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_xylosyltransferase Protein xylosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.26 2.4.2.26] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ejc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ejc OCA], [http://pdbe.org/6ejc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ejc RCSB], [http://www.ebi.ac.uk/pdbsum/6ejc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ejc ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ejc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ejc OCA], [https://pdbe.org/6ejc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ejc RCSB], [https://www.ebi.ac.uk/pdbsum/6ejc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ejc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/XYLT1_HUMAN 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. | + | [https://www.uniprot.org/uniprot/XYLT1_HUMAN 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 == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/XYLT1_HUMAN 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.<ref>PMID:15461586</ref> [[http://www.uniprot.org/uniprot/AMBP_HUMAN AMBP_HUMAN]] Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization.<ref>PMID:7676539</ref> Trypstatin is a trypsin inhibitor (By similarity).<ref>PMID:7676539</ref> | + | [https://www.uniprot.org/uniprot/XYLT1_HUMAN 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.<ref>PMID:15461586</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Protein xylosyltransferase]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Briggs, D C]] | + | [[Category: Large Structures]] |
| - | [[Category: Hohenester, E]] | + | [[Category: Briggs DC]] |
| - | [[Category: Glycosyltransferase]] | + | [[Category: Hohenester E]] |
| - | [[Category: Golgi]]
| + | |
| - | [[Category: Proteoglycan]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Xylosyltransferase]]
| + | |
| Structural highlights
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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Muller S, Schottler M, Schon S, Prante C, Brinkmann T, Kuhn J, Gotting C, Kleesiek K. Human xylosyltransferase I: functional and biochemical characterization of cysteine residues required for enzymic activity. Biochem J. 2005 Mar 1;386(Pt 2):227-36. PMID:15461586 doi:http://dx.doi.org/BJ20041206
- ↑ Briggs DC, Hohenester E. Structural Basis for the Initiation of Glycosaminoglycan Biosynthesis by Human Xylosyltransferase 1. Structure. 2018 Apr 10. pii: S0969-2126(18)30095-9. doi:, 10.1016/j.str.2018.03.014. PMID:29681470 doi:http://dx.doi.org/10.1016/j.str.2018.03.014
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