5kxq - Revision history

OCA at 11:00, 27 September 2023

2023-09-27T11:00:24Z

←Older revision		Revision as of 11:00, 27 September 2023
Line 3:		Line 3:
	<StructureSection load='5kxq' size='340' side='right'caption='[[5kxq]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='5kxq' size='340' side='right'caption='[[5kxq]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5kxq]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KXQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5KXQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5kxq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KXQ FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 1.9Å</td></tr>
-	~~<tr~~ id~~='related'><td class~~="~~sblockLbl~~">~~<b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5kxh\|5kxh]]~~, [[~~5ky0~~\|~~5ky0]], [[5ky2\|5ky2]], [[5ky3\|5ky3]], [[5ky4\|5ky4]], [[5ky5\|5ky5]], [[5ky7\|5ky7]], [[5ky8\|5ky8]], [[5ky9\|5ky9~~]]</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~Pofut1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=5~~&id=10090 LK3 transgenic mice])</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=5kxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kxq OCA], [https://pdbe.org/5kxq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kxq RCSB], [https://www.ebi.ac.uk/pdbsum/5kxq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kxq ProSAT]</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=5kxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kxq OCA], [~~http~~://pdbe.org/5kxq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5kxq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5kxq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5kxq ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== 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>	+	[https://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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lk3 transgenic mice]]~~	+	[[Category: Mus musculus]]
-	~~[[Category: Peptide-O-fucosyltransferase~~]]	+	[[Category: Li Z]]
-	[[Category: Li, Z]]	+	[[Category: Rini JM]]
-	[[Category: Rini~~, J M]]~~	+
-	~~[[Category: Glycosyltransferase o-fucosyltransferase gt-b inverting]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 08:12, 8 January 2020

2020-01-08T08:12:12Z

←Older revision		Revision as of 08:12, 8 January 2020
Line 1:		Line 1:

	==mouse POFUT1 in complex with GDP==		==mouse POFUT1 in complex with GDP==
-	<StructureSection load='5kxq' size='340' side='right' caption='[[5kxq]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='5kxq' size='340' side='right'caption='[[5kxq]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5kxq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KXQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KXQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5kxq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KXQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KXQ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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">[[5kxh\|5kxh]], [[5ky0\|5ky0]], [[5ky2\|5ky2]], [[5ky3\|5ky3]], [[5ky4\|5ky4]], [[5ky5\|5ky5]], [[5ky7\|5ky7]], [[5ky8\|5ky8]], [[5ky9\|5ky9]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5kxh\|5kxh]], [[5ky0\|5ky0]], [[5ky2\|5ky2]], [[5ky3\|5ky3]], [[5ky4\|5ky4]], [[5ky5\|5ky5]], [[5ky7\|5ky7]], [[5ky8\|5ky8]], [[5ky9\|5ky9]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Pofut1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=5kxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kxq OCA], [http://pdbe.org/5kxq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kxq RCSB], [http://www.ebi.ac.uk/pdbsum/5kxq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kxq ProSAT]</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=5kxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kxq OCA], [http://pdbe.org/5kxq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kxq RCSB], [http://www.ebi.ac.uk/pdbsum/5kxq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kxq ProSAT]</span></td></tr>
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Lk3 transgenic mice]]
	[[Category: Peptide-O-fucosyltransferase]]		[[Category: Peptide-O-fucosyltransferase]]
	[[Category: Li, Z]]		[[Category: Li, Z]]

OCA at 10:04, 3 August 2017

2017-08-03T10:04:02Z

←Older revision		Revision as of 10:04, 3 August 2017
Line 11:		Line 11:
	== Function ==		== 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/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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Protein O-fucosyltransferase 1 (POFUT1) fucosylates the epidermal growth factor (EGF)-like domains found in cell-surface and secreted glycoproteins including Notch and its ligands. Although Notch fucosylation is critical for development, and POFUT1 deficiency leads to human disease, how this enzyme binds and catalyzes the fucosylation of its diverse EGF-like domain substrates has not been determined. Reported here is the X-ray crystal structure of mouse POFUT1 in complex with several EGF-like domains, including EGF12 and EGF26 of Notch. Overall shape complementarity, interactions with invariant atoms of the fucosylation motif and flexible segments on POFUT1 all define its EGF-like-domain binding properties. Using large-scale structural and sequence analysis, we also show that POFUT1 binds EGF-like domains of the hEGF type and that the highly correlated presence of POFUT1 and fucosylatable hEGFs has accompanied animal evolution.
		+
		+	Recognition of EGF-like domains by the Notch-modifying O-fucosyltransferase POFUT1.,Li Z, Han K, Pak JE, Satkunarajah M, Zhou D, Rini JM Nat Chem Biol. 2017 Jul;13(7):757-763. doi: 10.1038/nchembio.2381. Epub 2017 May , 22. PMID:28530709<ref>PMID:28530709</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5kxq" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:47, 17 May 2017

2017-05-17T15:47:08Z

←Older revision		Revision as of 15:47, 17 May 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5kxq is ~~ON HOLD~~ ~~until Paper Publication~~	+	==mouse POFUT1 in complex with GDP==
-		+	<StructureSection load='5kxq' size='340' side='right' caption='[[5kxq]], [[Resolution\|resolution]] 1.90Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5kxq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KXQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KXQ FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5kxh\|5kxh]], [[5ky0\|5ky0]], [[5ky2\|5ky2]], [[5ky3\|5ky3]], [[5ky4\|5ky4]], [[5ky5\|5ky5]], [[5ky7\|5ky7]], [[5ky8\|5ky8]], [[5ky9\|5ky9]]</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=5kxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kxq OCA], [http://pdbe.org/5kxq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kxq RCSB], [http://www.ebi.ac.uk/pdbsum/5kxq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kxq 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>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Peptide-O-fucosyltransferase]]
		+	[[Category: Li, Z]]
		+	[[Category: Rini, J M]]
		+	[[Category: Glycosyltransferase o-fucosyltransferase gt-b inverting]]
		+	[[Category: Transferase]]

OCA at 13:52, 10 August 2016

2016-08-10T13:52:10Z

←Older revision		Revision as of 13:52, 10 August 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5kxq is ON HOLD	+	The entry 5kxq is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "5kxq" [edit=sysop:move=sysop]

2016-07-27T13:30:51Z

Protected "5kxq" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:30, 27 July 2016

OCA: New page: '''Unreleased structure''' The entry 5kxq is ON HOLD Authors: Description: Category: Unreleased Structures

2016-07-27T13:30:50Z

New page: '''Unreleased structure''' The entry 5kxq is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5kxq is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]