5cql - Revision history

OCA at 08:39, 27 September 2023

OCA — Wed, 27 Sep 2023 08:39:59 GMT

←Older revision		Revision as of 08:39, 27 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5cql]] is a 1 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=5CQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CQL FirstGlance]. <br>		<table><tr><td colspan='2'>[[5cql]] is a 1 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=5CQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CQL FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</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]] 1.69Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></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=5cql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cql OCA], [https://pdbe.org/5cql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cql RCSB], [https://www.ebi.ac.uk/pdbsum/5cql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cql 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=5cql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cql OCA], [https://pdbe.org/5cql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cql RCSB], [https://www.ebi.ac.uk/pdbsum/5cql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cql ProSAT]</span></td></tr>
	</table>		</table>

OCA at 12:24, 14 June 2023

OCA — Wed, 14 Jun 2023 12:24:12 GMT

←Older revision		Revision as of 12:24, 14 June 2023
Line 1:		Line 1:

	==GTB mutant with mercury - E303A==		==GTB mutant with mercury - E303A==
-	<StructureSection load='5cql' size='340' side='right' caption='[[5cql]], [[Resolution\|resolution]] 1.69Å' scene=''>	+	<StructureSection load='5cql' size='340' side='right'caption='[[5cql]], [[Resolution\|resolution]] 1.69Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5cql]] is a 1 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=5CQL OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5CQL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5cql]] is a 1 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=5CQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CQL FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5cmf\|5cmf]], [[5cmg\|5cmg]], [[5cmh\|5cmh]], [[5cmi\|5cmi]], [[5cmj\|5cmj]], [[5cqm\|5cqm]], [[5cqn\|5cqn]], [[5cqo\|5cqo]], [[5cqp\|5cqp]]</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=5cql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cql OCA], [https://pdbe.org/5cql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cql RCSB], [https://www.ebi.ac.uk/pdbsum/5cql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cql ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ABO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</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=5cql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cql OCA], [~~http~~://pdbe.org/5cql PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5cql RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5cql PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5cql ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/BGAT_HUMAN BGAT_HUMAN]] This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity.	+	[https://www.uniprot.org/uniprot/BGAT_HUMAN BGAT_HUMAN] This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 5cql" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5cql" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Glycosyltransferase 3D structures\|Glycosyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Blackler, R J~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Gagnon, S M.L~~]]	+	[[Category: Blackler RJ]]
-	[[Category: ~~Catalytic domain]]~~	+	[[Category: Gagnon SML]]
-	~~[[Category: Double turn motif]]~~	+
-	~~[[Category: Glycosyltransferase]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 06:03, 8 March 2018

OCA — Thu, 08 Mar 2018 06:03:25 GMT

←Older revision		Revision as of 06:03, 8 March 2018
Line 3:		Line 3:
	<StructureSection load='5cql' size='340' side='right' caption='[[5cql]], [[Resolution\|resolution]] 1.69Å' scene=''>		<StructureSection load='5cql' size='340' side='right' caption='[[5cql]], [[Resolution\|resolution]] 1.69Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5cql]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CQL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CQL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5cql]] is a 1 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=5CQL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CQL FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5cmf\|5cmf]], [[5cmg\|5cmg]], [[5cmh\|5cmh]], [[5cmi\|5cmi]], [[5cmj\|5cmj]], [[5cqm\|5cqm]], [[5cqn\|5cqn]], [[5cqo\|5cqo]], [[5cqp\|5cqp]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5cmf\|5cmf]], [[5cmg\|5cmg]], [[5cmh\|5cmh]], [[5cmi\|5cmi]], [[5cmj\|5cmj]], [[5cqm\|5cqm]], [[5cqn\|5cqn]], [[5cqo\|5cqo]], [[5cqp\|5cqp]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ABO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5cql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cql OCA], [http://pdbe.org/5cql PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cql RCSB], [http://www.ebi.ac.uk/pdbsum/5cql PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cql 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=5cql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cql OCA], [http://pdbe.org/5cql PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cql RCSB], [http://www.ebi.ac.uk/pdbsum/5cql PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cql ProSAT]</span></td></tr>
	</table>		</table>
Line 23:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Blackler, R J]]		[[Category: Blackler, R J]]
	[[Category: Gagnon, S M.L]]		[[Category: Gagnon, S M.L]]

OCA at 08:21, 18 January 2017

OCA — Wed, 18 Jan 2017 08:21:32 GMT

←Older revision		Revision as of 08:21, 18 January 2017
Line 10:		Line 10:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/BGAT_HUMAN BGAT_HUMAN]] This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity.		[[http://www.uniprot.org/uniprot/BGAT_HUMAN BGAT_HUMAN]] This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The homologous glycosyltransferases alpha-1,3-N-acetylgalactosaminyltransferase (GTA) and alpha-1,3-galactosyltransferase (GTB) carry out the final synthetic step of the closely related human ABO(H) blood group A and B antigens. The catalytic mechanism of these model retaining enzymes remains under debate, where Glu303 has been suggested to act as a putative nucleophile in a double displacement mechanism, a local dipole stabilizing the intermediate in an orthogonal associative mechanism or a general base to stabilize the reactive oxocarbenium ion-like intermediate in an S N i-like mechanism. Kinetic analysis of GTA and GTB point mutants E303C, E303D, E303Q and E303A shows that despite the enzymes having nearly identical sequences, the corresponding mutants of GTA/GTB have up to a 13-fold difference in their residual activities relative to wild type. High-resolution single crystal X-ray diffraction studies reveal, surprisingly, that the mutated Cys, Asp and Gln functional groups are no more than 0.8 A further from the anomeric carbon of donor substrate compared to wild type. However, complicating the analysis is the observation that Glu303 itself plays a critical role in maintaining the stability of a strained "double-turn" in the active site through several hydrogen bonds, and any mutation other than E303Q leads to significantly higher thermal motion or even disorder in the substrate recognition pockets. Thus, there is a remarkable juxtaposition of the mutants E303C and E303D, which retain significant activity despite disrupted active site architecture, with GTB/E303Q, which maintains active site architecture but exhibits zero activity. These findings indicate that nucleophilicity at position 303 is more catalytically valuable than active site stability and highlight the mechanistic elasticity of these enzymes.
		+
		+	Glycosyltransfer in mutants of putative catalytic residue Glu303 of the human ABO(H) A and B blood group glycosyltransferases GTA and GTB proceeds through a labile active site.,Blackler RJ, Gagnon SM, Polakowski R, Rose NL, Zheng RB, Letts JA, Johal AR, Schuman B, Borisova SN, Palcic MM, Evans SV Glycobiology. 2016 Nov 22. PMID:27979997<ref>PMID:27979997</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5cql" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 18:38, 26 October 2016

OCA — Wed, 26 Oct 2016 18:38:42 GMT

←Older revision		Revision as of 18:38, 26 October 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5cql is ~~ON HOLD until Oct 26 2017~~	+	==GTB mutant with mercury - E303A==
-		+	<StructureSection load='5cql' size='340' side='right' caption='[[5cql]], [[Resolution\|resolution]] 1.69Å' scene=''>
-	~~Authors~~: ~~Gagnon~~, S.M.L., ~~Blackler~~, R.J.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5cql]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CQL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CQL FirstGlance]. <br>
-	~~Description~~: ~~GTB mutant with mercury~~ -~~E303A~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5cmf\|5cmf]], [[5cmg\|5cmg]], [[5cmh\|5cmh]], [[5cmi\|5cmi]], [[5cmj\|5cmj]], [[5cqm\|5cqm]], [[5cqn\|5cqn]], [[5cqo\|5cqo]], [[5cqp\|5cqp]]</td></tr>
-	[[Category: Blackler, R.J]]	+	<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=5cql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cql OCA], [http://pdbe.org/5cql PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cql RCSB], [http://www.ebi.ac.uk/pdbsum/5cql PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cql ProSAT]</span></td></tr>
-	[[Category: Gagnon, S.M.L]]	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/BGAT_HUMAN BGAT_HUMAN]] This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity.
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Blackler, R J]]
		+	[[Category: Gagnon, S M.L]]
		+	[[Category: Catalytic domain]]
		+	[[Category: Double turn motif]]
		+	[[Category: Glycosyltransferase]]
		+	[[Category: Transferase]]

OCA at 08:59, 27 July 2016

OCA — Wed, 27 Jul 2016 08:59:18 GMT

←Older revision		Revision as of 08:59, 27 July 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5cql is ON HOLD until ~~Paper Publication~~	+	The entry 5cql is ON HOLD until Oct 26 2017

	Authors: Gagnon, S.M.L., Blackler, R.J.		Authors: Gagnon, S.M.L., Blackler, R.J.

OCA at 18:50, 5 August 2015

OCA — Wed, 05 Aug 2015 18:50:16 GMT

←Older revision		Revision as of 18:50, 5 August 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Gagnon, S.M.L., Blackler, R.J.		Authors: Gagnon, S.M.L., Blackler, R.J.

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

OCA — Wed, 29 Jul 2015 13:45:08 GMT

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

←Older revision

Revision as of 13:45, 29 July 2015

OCA: New page: '''Unreleased structure''' The entry 5cql is ON HOLD Authors: Gagnon, S.M.L., Blackler, R.J. Description: GTB mutant with mercury -E303A Category: Unreleased Structures [[Category:...

OCA — Wed, 29 Jul 2015 13:45:06 GMT

New page: '''Unreleased structure''' The entry 5cql is ON HOLD Authors: Gagnon, S.M.L., Blackler, R.J. Description: GTB mutant with mercury -E303A Category: Unreleased Structures [[Category:...

New page

'''Unreleased structure'''

The entry 5cql is ON HOLD

Authors: Gagnon, S.M.L., Blackler, R.J.

Description: GTB mutant with mercury -E303A
[[Category: Unreleased Structures]]
[[Category: Blackler, R.J]]
[[Category: Gagnon, S.M.L]]