4ap6
From Proteopedia
(Difference between revisions)
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==Crystal structure of human POFUT2 E54A mutant in complex with GDP- fucose== | ==Crystal structure of human POFUT2 E54A mutant in complex with GDP- fucose== | ||
<StructureSection load='4ap6' size='340' side='right' caption='[[4ap6]], [[Resolution|resolution]] 3.40Å' scene=''> | <StructureSection load='4ap6' size='340' side='right' caption='[[4ap6]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[4ap6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[4ap6]] is a 4 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=4AP6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AP6 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GFB:GUANOSINE-5-DIPHOSPHATE-BETA-L-FUCOPYRANOSE'>GFB</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GFB:GUANOSINE-5-DIPHOSPHATE-BETA-L-FUCOPYRANOSE'>GFB</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ap5|4ap5]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ap5|4ap5]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide-O-fucosyltransferase Peptide-O-fucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.221 2.4.1.221] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide-O-fucosyltransferase Peptide-O-fucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.221 2.4.1.221] </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=4ap6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ap6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ap6 RCSB], [http://www.ebi.ac.uk/pdbsum/4ap6 PDBsum]</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=4ap6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ap6 OCA], [http://pdbe.org/4ap6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ap6 RCSB], [http://www.ebi.ac.uk/pdbsum/4ap6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ap6 ProSAT]</span></td></tr> |
</table> | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/OFUT2_HUMAN OFUT2_HUMAN]] Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X(2,3)-S/T-C2-X(2)-G of thrombospondin type 1 repeats where C1 and C2 are the first and second cysteines, respectively. O-fucosylates members of several protein families including the ADAMTS family, the thrombosporin (TSP) and spondin families. The O-fucosylation of TSRs is also required for restricting epithelial to mesenchymal transition (EMT), maintaining the correct patterning of mesoderm and localization of the definite endoderm (By similarity). Required for the proper secretion of ADAMTS family members such as ADAMSL1 and ADAMST13.<ref>PMID:11067851</ref> <ref>PMID:16464858</ref> <ref>PMID:17395588</ref> <ref>PMID:17395589</ref> <ref>PMID:22588082</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
+ | <div class="pdbe-citations 4ap6" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Human]] |
[[Category: Peptide-O-fucosyltransferase]] | [[Category: Peptide-O-fucosyltransferase]] | ||
[[Category: Chen, C]] | [[Category: Chen, C]] |
Revision as of 12:07, 11 August 2016
Crystal structure of human POFUT2 E54A mutant in complex with GDP- fucose
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Categories: Human | Peptide-O-fucosyltransferase | Chen, C | Gut, H | Hess, D | Hofsteenge, J | Keusch, J J | Klein, D | Gt-b | Gt68 | Transferase