View source for 6ejc


==Human Xylosyltransferase 1 in complex with peptide QEEEGSGVGQGG==
<StructureSection load='6ejc' size='340' side='right'caption='[[6ejc]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.057&#8491;</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'>[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>
== Disease ==
[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 ==
[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;">
== 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<ref>PMID:29681470</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ejc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Briggs DC]]
[[Category: Hohenester E]]