7jhl - Revision history

OCA at 15:02, 18 October 2023

2023-10-18T15:02:55Z

←Older revision		Revision as of 15:02, 18 October 2023
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	<StructureSection load='7jhl' size='340' side='right'caption='[[7jhl]], [[Resolution\|resolution]] 2.26Å' scene=''>		<StructureSection load='7jhl' size='340' side='right'caption='[[7jhl]], [[Resolution\|resolution]] 2.26Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[7jhl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JHL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JHL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7jhl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JHL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JHL FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</scene~~>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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]] 2.26Å</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">B3GNT2, B3GALT7, B3GNT1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/N-acetyllactosaminide_beta-1,3-N-acetylglucosaminyltransferase N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.149 2.4.1.149] </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=7jhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jhl OCA], [https://pdbe.org/7jhl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jhl RCSB], [https://www.ebi.ac.uk/pdbsum/7jhl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jhl 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=7jhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jhl OCA], [https://pdbe.org/7jhl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jhl RCSB], [https://www.ebi.ac.uk/pdbsum/7jhl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jhl ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/B3GN2_HUMAN B3GN2_HUMAN]] Beta-1,3-N-acetylglucosaminyltransferase involved in the synthesis of poly-N-acetyllactosamine. Catalyzes the initiation and elongation of poly-N-acetyllactosamine chains. Shows a marked preference for Gal(beta1-4)Glc(NAc)-based acceptors (PubMed:9892646). Probably constitutes the main polylactosamine synthase.<ref>PMID:11042166</ref> <ref>PMID:25279697</ref> <ref>PMID:9892646</ref>	+	[https://www.uniprot.org/uniprot/B3GN2_HUMAN B3GN2_HUMAN] Beta-1,3-N-acetylglucosaminyltransferase involved in the synthesis of poly-N-acetyllactosamine. Catalyzes the initiation and elongation of poly-N-acetyllactosamine chains. Shows a marked preference for Gal(beta1-4)Glc(NAc)-based acceptors (PubMed:9892646). Probably constitutes the main polylactosamine synthase.<ref>PMID:11042166</ref> <ref>PMID:25279697</ref> <ref>PMID:9892646</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase]]~~	+	[[Category: Hao Y]]
-	[[Category: Hao, Y]]	+	[[Category: Huang X]]
-	[[Category: Huang, X]]	+
-	~~[[Category: Glycosyltransferase]]~~	+
-	~~[[Category: Poly-n-acetyl-lactosamine]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 10:07, 14 July 2021

2021-07-14T10:07:33Z

←Older revision		Revision as of 10:07, 14 July 2021
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	==Structure of human beta 1,3-N-acetylglucosaminyltransferase 2 with UDP-N-acetylglucosamine==		==Structure of human beta 1,3-N-acetylglucosaminyltransferase 2 with UDP-N-acetylglucosamine==
-	<StructureSection load='7jhl' size='340' side='right'caption='[[7jhl]]' scene=''>	+	<StructureSection load='7jhl' size='340' side='right'caption='[[7jhl]], [[Resolution\|resolution]] 2.26Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JHL OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=7JHL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7jhl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JHL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JHL FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=7jhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jhl OCA], [~~http~~://pdbe.org/7jhl PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=7jhl RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/7jhl PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=7jhl ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">B3GNT2, B3GALT7, B3GNT1 ([https://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'>[https://en.wikipedia.org/wiki/N-acetyllactosaminide_beta-1,3-N-acetylglucosaminyltransferase N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.149 2.4.1.149] </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=7jhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jhl OCA], [https://pdbe.org/7jhl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jhl RCSB], [https://www.ebi.ac.uk/pdbsum/7jhl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jhl ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[https://www.uniprot.org/uniprot/B3GN2_HUMAN B3GN2_HUMAN]] Beta-1,3-N-acetylglucosaminyltransferase involved in the synthesis of poly-N-acetyllactosamine. Catalyzes the initiation and elongation of poly-N-acetyllactosamine chains. Shows a marked preference for Gal(beta1-4)Glc(NAc)-based acceptors (PubMed:9892646). Probably constitutes the main polylactosamine synthase.<ref>PMID:11042166</ref> <ref>PMID:25279697</ref> <ref>PMID:9892646</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	beta1,3-N-acetylglucosaminyltransferases (B3GNTs) are Golgi-resident glycosyltransferases involved in the biosynthesis of poly-N-acetyl-lactosamine chains. They catalyze the addition of the N-acetylglucosamine to the N-acetyl-lactosamine repeat as a key step of the chain elongation process. Poly-N-acetyl-lactosamine is involved in immune system in many ways. Particularly, its long chain has been demonstrated to suppress excessive immune responses. Among the characterized B3GNTs, B3GNT2 is the major poly-N-acetyl-lactosamine synthase and deletion of its coding gene dramatically reduced the cell surface poly-N-acetyl-lactosamine and led to hypersensitive and hyperresponsive immunocytes. Despite the extensive functional studies, no structural information is available to understand the molecular mechanism of B3GNT2, as well as other B3GNTs. Here we present the structural and kinetic studies of the human B3GNT2. Five crystal structures of B3GNT2 have been determined in the unliganded, donor substrate-bound, acceptor substrate-bound and product(s)-bound states at resolutions ranging from 1.85 A to 2.35 A. Kinetic study shows that the transglycosylation reaction follows a sequential mechanism. Critical residues involved in recognition of both donor and acceptor substrates as well as catalysis are identified. Mutations of these invariant residues impair B3GNT2 activity in cell assays. Structural comparison with other glycosyltransferases such as mouse Fringe reveals a novel N-terminal helical domain of B3GNTs that may stabilize the catalytic domain and distinguish among different acceptor substrates.
		+
		+	Structures and mechanism of human glycosyltransferase beta1,3-N-acetylglucosaminyltransferase 2 (B3GNT2), an important player in immune homeostasis.,Hao Y, Crequer-Grandhomme A, Javier N, Singh A, Chen H, Manzanillo P, Lo MC, Huang X J Biol Chem. 2020 Nov 6. pii: RA120.015306. doi: 10.1074/jbc.RA120.015306. PMID:33158990<ref>PMID:33158990</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7jhl" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Hao Y]]	+	[[Category: N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase]]
-	[[Category: Huang X]]	+	[[Category: Hao, Y]]
		+	[[Category: Huang, X]]
		+	[[Category: Glycosyltransferase]]
		+	[[Category: Poly-n-acetyl-lactosamine]]
		+	[[Category: Transferase]]

OCA at 09:41, 18 November 2020

2020-11-18T09:41:36Z

←Older revision		Revision as of 09:41, 18 November 2020
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-	'''Unreleased structure'''

-	~~The entry~~ 7jhl ~~is ON HOLD until Paper Publication~~	+	==Structure of human beta 1,3-N-acetylglucosaminyltransferase 2 with UDP-N-acetylglucosamine==
-		+	<StructureSection load='7jhl' size='340' side='right'caption='[[7jhl]]' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JHL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7JHL FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7jhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jhl OCA], [http://pdbe.org/7jhl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7jhl RCSB], [http://www.ebi.ac.uk/pdbsum/7jhl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7jhl ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Hao Y]]
		+	[[Category: Huang X]]

OCA at 09:32, 26 August 2020

2020-08-26T09:32:44Z

←Older revision		Revision as of 09:32, 26 August 2020
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 7jhl is ON HOLD	+	The entry 7jhl is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "7jhl" [edit=sysop:move=sysop]

2020-07-29T09:50:06Z

Protected "7jhl" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:50, 29 July 2020

OCA: New page: '''Unreleased structure''' The entry 7jhl is ON HOLD Authors: Description: Category: Unreleased Structures

2020-07-29T09:50:05Z

New page: '''Unreleased structure''' The entry 7jhl is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 7jhl is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]