4pxq: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4pxq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PXQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[4pxq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PXQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IDS:2-O-SULFO-ALPHA-L-IDOPYRANURONIC+ACID'>IDS</scene>, <scene name='pdbligand=SGN:N,O6-DISULFO-GLUCOSAMINE'>SGN</scene>, <scene name='pdbligand=UAP:4-DEOXY-2-O-SULFO-ALPHA-L-THREO-HEX-4-ENOPYRANURONIC+ACID'>UAP</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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IDS:2-O-SULFO-ALPHA-L-IDOPYRANURONIC+ACID'>IDS</scene>, <scene name='pdbligand=SGN:N,O6-DISULFO-GLUCOSAMINE'>SGN</scene>, <scene name='pdbligand=UAP:4-DEOXY-2-O-SULFO-ALPHA-L-THREO-HEX-4-ENOPYRANURONIC+ACID'>UAP</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=4pxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pxq OCA], [https://pdbe.org/4pxq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pxq RCSB], [https://www.ebi.ac.uk/pdbsum/4pxq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pxq 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=4pxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pxq OCA], [https://pdbe.org/4pxq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pxq RCSB], [https://www.ebi.ac.uk/pdbsum/4pxq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pxq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/GLCEB_DANRE GLCEB_DANRE] Converts D-glucuronic acid residues adjacent to N-sulfate sugar residues to L-iduronic acid residues, both in maturing heparan sulfate (HS) and heparin chains (PubMed:16156897, PubMed:25568314). Plays a role in dorso-ventral axis specification during early development, together with glcea, where it may potentiate signaling via the BMP pathway (PubMed:16156897).<ref>PMID:16156897</ref> <ref>PMID:25568314</ref>  
[https://www.uniprot.org/uniprot/GLCEB_DANRE GLCEB_DANRE] Converts D-glucuronic acid residues adjacent to N-sulfate sugar residues to L-iduronic acid residues, both in maturing heparan sulfate (HS) and heparin chains (PubMed:16156897, PubMed:25568314). Plays a role in dorso-ventral axis specification during early development, together with glcea, where it may potentiate signaling via the BMP pathway (PubMed:16156897).<ref>PMID:16156897</ref> <ref>PMID:25568314</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Heparan sulfate (HS) is a glycosaminoglycan present on the cell surface and in the extracellular matrix which interacts with diverse signal molecules and is essential for many physiological processes including embryonic development, cell growth, inflammation, and blood coagulation. D-glucuronyl C5-epimerase (Glce) is a crucial enzyme in HS synthesis, converting D-glucuronic acid (GlcA) to L-iduronic acid (IdoA) to increase HS flexibility. This modification of HS is important for protein ligand recognition. We have determined the crystal structures of Glce in apo form (unliganded) and in complex with heparin hexasaccharide (product of Glce following O-sulfation), both in a stable dimer conformation. A Glce dimer contains two catalytic sites, each at a positively charged cleft in C-terminal alpha-helical domains binding one negatively charged hexasaccharide. Based on the structural and mutagenesis studies, three tyrosine residues, Y468, Y528, and Y546 in the active site were found to be crucial for the enzymatic activity. The complex structure also reveals the mechanism of product inhibition, i.e. 2-O- and 6-O-sulfation of HS keeps the C5 carbon of IdoA away from the active-site tyrosine residues. Our structural and functional data advance understanding of the key modification regulation in HS biosynthesis.
Structural and functional study of D-glucuronyl C5-epimerase.,Qin Y, Ke J, Gu X, Fang J, Wang W, Cong Q, Li J, Tan J, Brunzelle JS, Zhang C, Jiang Y, Melcher K, Li JP, Xu HE, Ding K J Biol Chem. 2015 Jan 7. pii: jbc.M114.602201. PMID:25568314<ref>PMID:25568314</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4pxq" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Latest revision as of 15:43, 1 March 2024

Crystal structure of D-glucuronyl C5-epimerase in complex with heparin hexasaccharideCrystal structure of D-glucuronyl C5-epimerase in complex with heparin hexasaccharide

Structural highlights

4pxq is a 2 chain structure with sequence from Danio rerio. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GLCEB_DANRE Converts D-glucuronic acid residues adjacent to N-sulfate sugar residues to L-iduronic acid residues, both in maturing heparan sulfate (HS) and heparin chains (PubMed:16156897, PubMed:25568314). Plays a role in dorso-ventral axis specification during early development, together with glcea, where it may potentiate signaling via the BMP pathway (PubMed:16156897).[1] [2]

References

  1. ↑ Ghiselli G, Farber SA. D-glucuronyl C5-epimerase acts in dorso-ventral axis formation in zebrafish. BMC Dev Biol. 2005 Sep 12;5:19. PMID:16156897 doi:10.1186/1471-213X-5-19
  2. ↑ Qin Y, Ke J, Gu X, Fang J, Wang W, Cong Q, Li J, Tan J, Brunzelle JS, Zhang C, Jiang Y, Melcher K, Li JP, Xu HE, Ding K. Structural and functional study of D-glucuronyl C5-epimerase. J Biol Chem. 2015 Jan 7. pii: jbc.M114.602201. PMID:25568314 doi:http://dx.doi.org/10.1074/jbc.M114.602201

4pxq, resolution 2.20Å

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