1v83 - Revision history

OCA at 07:49, 25 October 2023

OCA — Wed, 25 Oct 2023 07:49:53 GMT

←Older revision		Revision as of 07:49, 25 October 2023
Line 3:		Line 3:
	<StructureSection load='1v83' size='340' side='right'caption='[[1v83]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1v83' size='340' side='right'caption='[[1v83]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1v83]] 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=1V83 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V83 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1v83]] 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=1V83 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V83 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TLA:L(+)~~-~~TARTARIC+ACID'>TLA</scene>~~, ~~<scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</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"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1v82\|1v82]], [[1v84\|1v84]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks'>[https~~:~~//en.wikipedia.org/wiki/Galactosylgalactosylxylosylprotein_3~~-~~beta~~-~~glucuronosyltransferase Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.135 2.4.1.135]~~ </~~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=1v83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v83 OCA], [https://pdbe.org/1v83 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v83 RCSB], [https://www.ebi.ac.uk/pdbsum/1v83 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v83 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=1v83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v83 OCA], [https://pdbe.org/1v83 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v83 RCSB], [https://www.ebi.ac.uk/pdbsum/1v83 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v83 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/B3GA1_HUMAN B3GA1_HUMAN]] Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on glycoproteins. Can also play a role in glycosaminoglycan biosynthesis. Substrates include asialo-orosomucoid (ASOR), asialo-fetuin, and asialo-neural cell adhesion molecule. Requires sphingomyelin for activity: stearoyl-sphingomyelin was the most effective, followed by palmitoyl-sphingomyelin and lignoceroyl-sphingomyelin. Activity was demonstrated only for sphingomyelin with a saturated fatty acid and not for that with an unsaturated fatty acid, regardless of the length of the acyl group (By similarity).	+	[https://www.uniprot.org/uniprot/B3GA1_HUMAN B3GA1_HUMAN] Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on glycoproteins. Can also play a role in glycosaminoglycan biosynthesis. Substrates include asialo-orosomucoid (ASOR), asialo-fetuin, and asialo-neural cell adhesion molecule. Requires sphingomyelin for activity: stearoyl-sphingomyelin was the most effective, followed by palmitoyl-sphingomyelin and lignoceroyl-sphingomyelin. Activity was demonstrated only for sphingomyelin with a saturated fatty acid and not for that with an unsaturated fatty acid, regardless of the length of the acyl group (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Ishiguro, M]]	+	[[Category: Ishiguro M]]
-	[[Category: Kajihara, Y]]	+	[[Category: Kajihara Y]]
-	[[Category: Kakuda, S]]	+	[[Category: Kakuda S]]
-	[[Category: Kato, R]]	+	[[Category: Kato R]]
-	[[Category: Kawasaki, T]]	+	[[Category: Kawasaki T]]
-	[[Category: Oka, S]]	+	[[Category: Oka S]]
-	[[Category: Shiba, T]]	+	[[Category: Shiba T]]
-	[[Category: Tagawa, H]]	+	[[Category: Tagawa H]]
-	[[Category: Wakatsuki, S]]	+	[[Category: Wakatsuki S]]
-	~~[[Category: Glycocyltransferase]]~~	+
-	~~[[Category: Glycoprotein]]~~	+
-	~~[[Category: Hnk-1 epitope]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 06:27, 6 October 2021

OCA — Wed, 06 Oct 2021 06:27:11 GMT

←Older revision		Revision as of 06:27, 6 October 2021
Line 3:		Line 3:
	<StructureSection load='1v83' size='340' side='right'caption='[[1v83]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1v83' size='340' side='right'caption='[[1v83]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1v83]] is a 2 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=1V83 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1V83 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1v83]] 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=1V83 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V83 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1v82\|1v82]], [[1v84\|1v84]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1v82\|1v82]], [[1v84\|1v84]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Galactosylgalactosylxylosylprotein_3-beta-glucuronosyltransferase Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.135 2.4.1.135] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Galactosylgalactosylxylosylprotein_3-beta-glucuronosyltransferase Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.135 2.4.1.135] </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=1v83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v83 OCA], [~~http~~://pdbe.org/1v83 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1v83 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1v83 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1v83 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=1v83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v83 OCA], [https://pdbe.org/1v83 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v83 RCSB], [https://www.ebi.ac.uk/pdbsum/1v83 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v83 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/B3GA1_HUMAN B3GA1_HUMAN]] Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on glycoproteins. Can also play a role in glycosaminoglycan biosynthesis. Substrates include asialo-orosomucoid (ASOR), asialo-fetuin, and asialo-neural cell adhesion molecule. Requires sphingomyelin for activity: stearoyl-sphingomyelin was the most effective, followed by palmitoyl-sphingomyelin and lignoceroyl-sphingomyelin. Activity was demonstrated only for sphingomyelin with a saturated fatty acid and not for that with an unsaturated fatty acid, regardless of the length of the acyl group (By similarity).	+	[[https://www.uniprot.org/uniprot/B3GA1_HUMAN B3GA1_HUMAN]] Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on glycoproteins. Can also play a role in glycosaminoglycan biosynthesis. Substrates include asialo-orosomucoid (ASOR), asialo-fetuin, and asialo-neural cell adhesion molecule. Requires sphingomyelin for activity: stearoyl-sphingomyelin was the most effective, followed by palmitoyl-sphingomyelin and lignoceroyl-sphingomyelin. Activity was demonstrated only for sphingomyelin with a saturated fatty acid and not for that with an unsaturated fatty acid, regardless of the length of the acyl group (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 13:10, 1 January 2020

OCA — Wed, 01 Jan 2020 13:10:47 GMT

←Older revision		Revision as of 13:10, 1 January 2020
Line 1:		Line 1:

	==Crystal structure of human GlcAT-P in complex with Udp and Mn2+==		==Crystal structure of human GlcAT-P in complex with Udp and Mn2+==
-	<StructureSection load='1v83' size='340' side='right' caption='[[1v83]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='1v83' size='340' side='right'caption='[[1v83]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1v83]] is a 2 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=1V83 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V83 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1v83]] is a 2 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=1V83 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V83 FirstGlance]. <br>
Line 36:		Line 36:
	[[Category: Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase]]		[[Category: Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Ishiguro, M]]		[[Category: Ishiguro, M]]
	[[Category: Kajihara, Y]]		[[Category: Kajihara, Y]]

OCA at 08:00, 28 March 2018

OCA — Wed, 28 Mar 2018 08:00:43 GMT

←Older revision		Revision as of 08:00, 28 March 2018
Line 1:		Line 1:
		+
	==Crystal structure of human GlcAT-P in complex with Udp and Mn2+==		==Crystal structure of human GlcAT-P in complex with Udp and Mn2+==
	<StructureSection load='1v83' size='340' side='right' caption='[[1v83]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1v83' size='340' side='right' caption='[[1v83]], [[Resolution\|resolution]] 1.90Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1v82\|1v82]], [[1v84\|1v84]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1v82\|1v82]], [[1v84\|1v84]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Galactosylgalactosylxylosylprotein_3-beta-glucuronosyltransferase Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.135 2.4.1.135] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Galactosylgalactosylxylosylprotein_3-beta-glucuronosyltransferase Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.135 2.4.1.135] </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=1v83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v83 OCA], [http://pdbe.org/1v83 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v83 RCSB], [http://www.ebi.ac.uk/pdbsum/1v83 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=1v83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v83 OCA], [http://pdbe.org/1v83 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v83 RCSB], [http://www.ebi.ac.uk/pdbsum/1v83 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1v83 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v8/1v83_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v8/1v83_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 20:48, 9 February 2016

OCA — Tue, 09 Feb 2016 20:48:51 GMT

←Older revision		Revision as of 20:48, 9 February 2016
Line 18:		Line 18:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1v83 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 01:54, 11 September 2015

OCA — Fri, 11 Sep 2015 01:54:31 GMT

←Older revision		Revision as of 01:54, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1v83' size='340' side='right' caption='[[1v83]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1v83' size='340' side='right' caption='[[1v83]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1v83]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V83 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V83 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1v83]] is a 2 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=1V83 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V83 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1v82\|1v82]], [[1v84\|1v84]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1v82\|1v82]], [[1v84\|1v84]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Galactosylgalactosylxylosylprotein_3-beta-glucuronosyltransferase Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.135 2.4.1.135] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Galactosylgalactosylxylosylprotein_3-beta-glucuronosyltransferase Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.135 2.4.1.135] </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=1v83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v83 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1v83 RCSB], [http://www.ebi.ac.uk/pdbsum/1v83 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=1v83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v83 OCA], [http://pdbe.org/1v83 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v83 RCSB], [http://www.ebi.ac.uk/pdbsum/1v83 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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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 1v83" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 33:		Line 34:
	</StructureSection>		</StructureSection>
	[[Category: Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase]]		[[Category: Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Ishiguro, M]]		[[Category: Ishiguro, M]]
	[[Category: Kajihara, Y]]		[[Category: Kajihara, Y]]

OCA at 09:26, 25 December 2014

OCA — Thu, 25 Dec 2014 09:26:29 GMT

←Older revision		Revision as of 09:26, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1v83]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V83 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V83 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1v83]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V83 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V83 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1v82\|1v82]], [[1v84\|1v84]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1v82\|1v82]], [[1v84\|1v84]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Galactosylgalactosylxylosylprotein_3-beta-glucuronosyltransferase Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.135 2.4.1.135] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Galactosylgalactosylxylosylprotein_3-beta-glucuronosyltransferase Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.135 2.4.1.135] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v83 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1v83 RCSB], [http://www.ebi.ac.uk/pdbsum/1v83 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=1v83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v83 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1v83 RCSB], [http://www.ebi.ac.uk/pdbsum/1v83 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/B3GA1_HUMAN B3GA1_HUMAN]] Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on glycoproteins. Can also play a role in glycosaminoglycan biosynthesis. Substrates include asialo-orosomucoid (ASOR), asialo-fetuin, and asialo-neural cell adhesion molecule. Requires sphingomyelin for activity: stearoyl-sphingomyelin was the most effective, followed by palmitoyl-sphingomyelin and lignoceroyl-sphingomyelin. Activity was demonstrated only for sphingomyelin with a saturated fatty acid and not for that with an unsaturated fatty acid, regardless of the length of the acyl group (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 34:
	[[Category: Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase]]		[[Category: Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Ishiguro, M.]]	+	[[Category: Ishiguro, M]]
-	[[Category: Kajihara, Y.]]	+	[[Category: Kajihara, Y]]
-	[[Category: Kakuda, S.]]	+	[[Category: Kakuda, S]]
-	[[Category: Kato, R.]]	+	[[Category: Kato, R]]
-	[[Category: Kawasaki, T.]]	+	[[Category: Kawasaki, T]]
-	[[Category: Oka, S.]]	+	[[Category: Oka, S]]
-	[[Category: Shiba, T.]]	+	[[Category: Shiba, T]]
-	[[Category: Tagawa, H.]]	+	[[Category: Tagawa, H]]
-	[[Category: Wakatsuki, S.]]	+	[[Category: Wakatsuki, S]]
	[[Category: Glycocyltransferase]]		[[Category: Glycocyltransferase]]
	[[Category: Glycoprotein]]		[[Category: Glycoprotein]]
	[[Category: Hnk-1 epitope]]		[[Category: Hnk-1 epitope]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 20:34, 29 September 2014

OCA — Mon, 29 Sep 2014 20:34:58 GMT

←Older revision		Revision as of 20:34, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1v83.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of human GlcAT-P in complex with Udp and Mn2+==
		+	<StructureSection load='1v83' size='340' side='right' caption='[[1v83]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1v83]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V83 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V83 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1v82\|1v82]], [[1v84\|1v84]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Galactosylgalactosylxylosylprotein_3-beta-glucuronosyltransferase Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.135 2.4.1.135] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v83 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1v83 RCSB], [http://www.ebi.ac.uk/pdbsum/1v83 PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v8/1v83_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The HNK-1 carbohydrate epitope is found on many neural cell adhesion molecules. Its structure is characterized by a terminal sulfated glucuronyl acid. The glucuronyltransferases, GlcAT-P and GlcAT-S, are involved in the biosynthesis of the HNK-1 epitope, GlcAT-P as the major enzyme. We overexpressed and purified the recombinant human GlcAT-P from Escherichia coli. Analysis of its enzymatic activity showed that it catalyzed the transfer reaction for N-acetyllactosamine (Galbeta1-4GlcNAc) but not lacto-N-biose (Galbeta1-3GlcNAc) as an acceptor substrate. Subsequently, we determined the first x-ray crystal structures of human GlcAT-P, in the absence and presence of a donor substrate product UDP, catalytic Mn(2+), and an acceptor substrate analogue N-acetyllactosamine (Galbeta1-4GlcNAc) or an asparagine-linked biantennary nonasaccharide. The asymmetric unit contains two independent molecules. Each molecule is an alpha/beta protein with two regions that constitute the donor and acceptor substrate binding sites. The UDP moiety of donor nucleotide sugar is recognized by conserved amino acid residues including a DXD motif (Asp(195)-Asp(196)-Asp(197)). Other conserved amino acid residues interact with the terminal galactose moiety of the acceptor substrate. In addition, Val(320) and Asn(321), which are located on the C-terminal long loop from a neighboring molecule, and Phe(245) contribute to the interaction with GlcNAc moiety. These three residues play a key role in establishing the acceptor substrate specificity.

-	~~{{STRUCTURE_1v83\| PDB=1v83 \| SCENE= }}~~	+	Structural basis for acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1.,Kakuda S, Shiba T, Ishiguro M, Tagawa H, Oka S, Kajihara Y, Kawasaki T, Wakatsuki S, Kato R J Biol Chem. 2004 May 21;279(21):22693-703. Epub 2004 Mar 1. PMID:14993226<ref>PMID:14993226</ref>

-	~~===Crystal structure~~ of ~~human GlcAT-P in complex with Udp and Mn2+===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_14993226}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1v83]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1V83 OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:014993226<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase]]		[[Category: Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA: Protected "1v83" [edit=sysop:move=sysop]

OCA — Sat, 05 Jan 2013 11:19:57 GMT

Protected "1v83" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:19, 5 January 2013

OCA at 11:19, 5 January 2013

OCA — Sat, 05 Jan 2013 11:19:56 GMT

←Older revision		Revision as of 11:19, 5 January 2013
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1v83.png\|left\|200px]]		[[Image:1v83.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1v83", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1v83\| PDB=1v83 \| SCENE= }}		{{STRUCTURE_1v83\| PDB=1v83 \| SCENE= }}

	===Crystal structure of human GlcAT-P in complex with Udp and Mn2+===		===Crystal structure of human GlcAT-P in complex with Udp and Mn2+===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_14993226}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 14993226 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_14993226}}		{{ABSTRACT_PUBMED_14993226}}

	==About this Structure==		==About this Structure==
-	~~1V83~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V83 OCA].	+	[[1v83]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V83 OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~14993226~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:014993226</ref><references group="xtra"/>
	[[Category: Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase]]		[[Category: Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
Line 39:		Line 27:
	[[Category: Hnk-1 epitope]]		[[Category: Hnk-1 epitope]]
	[[Category: Transferase]]		[[Category: Transferase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 12:38:43 2009''