5ky2
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==mouse POFUT1 in complex with O-glucosylated mouse Factor VII EGF1 and GDP== | |
| - | + | <StructureSection load='5ky2' size='340' side='right' caption='[[5ky2]], [[Resolution|resolution]] 1.47Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5ky2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KY2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KY2 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |
| - | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5khx|5khx]], [[5kxq|5kxq]], [[5kx0|5kx0]], [[5kx3|5kx3]], [[5kx4|5kx4]], [[5kx7|5kx7]], [[5kx8|5kx8]], [[5kx9|5kx9]]</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=5ky2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ky2 OCA], [http://pdbe.org/5ky2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ky2 RCSB], [http://www.ebi.ac.uk/pdbsum/5ky2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ky2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/OFUT1_MOUSE OFUT1_MOUSE]] Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Specifically uses GDP-fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer. Plays a crucial role in NOTCH signaling. Initial fucosylation of NOTCH by POFUT1 generates a substrate for FRINGE/RFNG, an acetylglucosaminyltransferase that can then extend the fucosylation on the NOTCH EGF repeats. This extended fucosylation is required for optimal ligand binding and canonical NOTCH signaling induced by DLL1 or JAGGED1. Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs).<ref>PMID:12697902</ref> <ref>PMID:18775496</ref> [[http://www.uniprot.org/uniprot/FA7_MOUSE FA7_MOUSE]] Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium (By similarity). | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Peptide-O-fucosyltransferase]] | ||
| + | [[Category: Li, Z]] | ||
| + | [[Category: Rini, J M]] | ||
| + | [[Category: Glycosyltransferase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 15:47, 17 May 2017
mouse POFUT1 in complex with O-glucosylated mouse Factor VII EGF1 and GDP
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