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6eje

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Human Xylosyltransferase 1 in complex with peptide PAAEGSGEQDFT

Structural highlights

6eje is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	XYLT1, XT1 (HUMAN)
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.^[1] [SDC1_HUMAN] Cell surface proteoglycan that bears both heparan sulfate and chondroitin sulfate and that links the cytoskeleton to the interstitial matrix.

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

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6eje"

@@ Line 3: / Line 3: @@
 <StructureSection load='6eje' size='340' side='right' caption='[[6eje]], [[Resolution|resolution]] 2.43&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6eje]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EJE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EJE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6eje]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EJE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EJE 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>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XYLT1, XT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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='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=6eje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eje OCA], [http://pdbe.org/6eje PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eje RCSB], [http://www.ebi.ac.uk/pdbsum/6eje PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eje ProSAT]</span></td></tr>
@@ Line 25: / Line 26: @@
 __TOC__
 </StructureSection>
+[[Category: Human]]
 [[Category: Protein xylosyltransferase]]
 [[Category: Briggs, D C]]

6eje

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Current revision

Human Xylosyltransferase 1 in complex with peptide PAAEGSGEQDFT

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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