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6foa

From Proteopedia

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Human Xylosyltransferase 1 apo structure

Structural highlights

6foa is a 1 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]

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/6foa"

@@ Line 3: / Line 3: @@
 <StructureSection load='6foa' size='340' side='right' caption='[[6foa]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
 == Structural highlights ==
-<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>
+<table><tr><td colspan='2'>[[6foa]] is a 1 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=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>
 </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>
+<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=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>
@@ Line 25: / Line 26: @@
 __TOC__
 </StructureSection>
+[[Category: Human]]
 [[Category: Protein xylosyltransferase]]
 [[Category: Briggs, D C]]

6foa

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Current revision

Human Xylosyltransferase 1 apo structure

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

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