6foa

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m (Protected "6foa" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6foa is ON HOLD
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==Human Xylosyltransferase 1 apo structure==
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<StructureSection load='6foa' size='340' side='right' caption='[[6foa]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6foa]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FOA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FOA FirstGlance]. <br>
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</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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<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>
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<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=6foa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6foa OCA], [http://pdbe.org/6foa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6foa RCSB], [http://www.ebi.ac.uk/pdbsum/6foa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6foa ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[[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.
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== Function ==
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[[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6foa" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Protein xylosyltransferase]]
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[[Category: Briggs, D C]]
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[[Category: Hohenester, E]]
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[[Category: Glycosyltransferase]]
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[[Category: Golgi]]
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[[Category: Proteoglycan]]
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[[Category: Transferase]]
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[[Category: Xylosyltransferase]]

Revision as of 08:16, 2 May 2018

Human Xylosyltransferase 1 apo structure

6foa, resolution 1.87Å

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