5cmg - Revision history

OCA at 08:39, 27 September 2023

OCA — Wed, 27 Sep 2023 08:39:12 GMT

←Older revision		Revision as of 08:39, 27 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5cmg]] 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=5CMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CMG FirstGlance]. <br>		<table><tr><td colspan='2'>[[5cmg]] 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=5CMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CMG 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]] 1.83Å</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=5cmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cmg OCA], [https://pdbe.org/5cmg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cmg RCSB], [https://www.ebi.ac.uk/pdbsum/5cmg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cmg 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=5cmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cmg OCA], [https://pdbe.org/5cmg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cmg RCSB], [https://www.ebi.ac.uk/pdbsum/5cmg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cmg ProSAT]</span></td></tr>
	</table>		</table>

OCA at 12:16, 14 June 2023

OCA — Wed, 14 Jun 2023 12:16:13 GMT

←Older revision		Revision as of 12:16, 14 June 2023
Line 1:		Line 1:

	==GTA mutant with mercury- E303C==		==GTA mutant with mercury- E303C==
-	<StructureSection load='5cmg' size='340' side='right' caption='[[5cmg]], [[Resolution\|resolution]] 1.83Å' scene=''>	+	<StructureSection load='5cmg' size='340' side='right'caption='[[5cmg]], [[Resolution\|resolution]] 1.83Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5cmg]] 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=5CMG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5CMG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5cmg]] 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=5CMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CMG 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]], [[5cmh\|5cmh]], [[5cmi\|5cmi]], [[5cmj\|5cmj]], [[5cql\|5cql]], [[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=5cmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cmg OCA], [https://pdbe.org/5cmg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cmg RCSB], [https://www.ebi.ac.uk/pdbsum/5cmg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cmg 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=5cmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cmg OCA], [~~http~~://pdbe.org/5cmg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5cmg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5cmg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5cmg 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 ==
Line 20:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 5cmg" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5cmg" 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~~]]	+	[[Category: Blackler RJ]]
-	[[Category: ~~Double turn motif]]~~	+	[[Category: Gagnon SM]]
-	~~[[Category: Glycosyltransferase]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 06:03, 8 March 2018

OCA — Thu, 08 Mar 2018 06:03:07 GMT

←Older revision		Revision as of 06:03, 8 March 2018
Line 3:		Line 3:
	<StructureSection load='5cmg' size='340' side='right' caption='[[5cmg]], [[Resolution\|resolution]] 1.83Å' scene=''>		<StructureSection load='5cmg' size='340' side='right' caption='[[5cmg]], [[Resolution\|resolution]] 1.83Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5cmg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CMG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CMG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5cmg]] 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=5CMG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CMG 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]], [[5cmh\|5cmh]], [[5cmi\|5cmi]], [[5cmj\|5cmj]], [[5cql\|5cql]], [[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]], [[5cmh\|5cmh]], [[5cmi\|5cmi]], [[5cmj\|5cmj]], [[5cql\|5cql]], [[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=5cmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cmg OCA], [http://pdbe.org/5cmg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cmg RCSB], [http://www.ebi.ac.uk/pdbsum/5cmg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cmg 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=5cmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cmg OCA], [http://pdbe.org/5cmg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cmg RCSB], [http://www.ebi.ac.uk/pdbsum/5cmg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cmg 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]]		[[Category: Gagnon, S M]]

OCA at 07:36, 18 January 2017

OCA — Wed, 18 Jan 2017 07:36:37 GMT

←Older revision		Revision as of 07:36, 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 5cmg" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 15:28, 26 July 2016

OCA — Tue, 26 Jul 2016 15:28:29 GMT

←Older revision		Revision as of 15:28, 26 July 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5cmg is ~~ON HOLD until Paper Publication~~	+	==GTA mutant with mercury- E303C==
-		+	<StructureSection load='5cmg' size='340' side='right' caption='[[5cmg]], [[Resolution\|resolution]] 1.83Å' scene=''>
-	~~Authors~~: ~~Gagnon~~, S.M., ~~Blackler~~, R.J.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5cmg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CMG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CMG FirstGlance]. <br>
-	~~Description~~: ~~GTA mutant with mercury~~-~~E303C~~	+	</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]], [[5cmh\|5cmh]], [[5cmi\|5cmi]], [[5cmj\|5cmj]], [[5cql\|5cql]], [[5cqm\|5cqm]], [[5cqn\|5cqn]], [[5cqo\|5cqo]], [[5cqp\|5cqp]]</td></tr>
-	[[Category: Gagnon, S.M]]	+	<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=5cmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cmg OCA], [http://pdbe.org/5cmg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cmg RCSB], [http://www.ebi.ac.uk/pdbsum/5cmg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cmg ProSAT]</span></td></tr>
-	[[Category: ~~Blackler, R.J~~]]	+	</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]]
		+	[[Category: Double turn motif]]
		+	[[Category: Glycosyltransferase]]
		+	[[Category: Transferase]]

OCA at 13:34, 29 July 2015

OCA — Wed, 29 Jul 2015 13:34:16 GMT

←Older revision		Revision as of 13:34, 29 July 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

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

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

OCA — Wed, 22 Jul 2015 13:21:08 GMT

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

←Older revision

Revision as of 13:21, 22 July 2015

OCA: New page: '''Unreleased structure''' The entry 5cmg is ON HOLD Authors: Gagnon, S.M., Blackler, R.J. Description: GTA mutant with mercury-E303C Category: Unreleased Structures [[Category: Ga...

OCA — Wed, 22 Jul 2015 13:21:07 GMT

New page: '''Unreleased structure''' The entry 5cmg is ON HOLD Authors: Gagnon, S.M., Blackler, R.J. Description: GTA mutant with mercury-E303C Category: Unreleased Structures [[Category: Ga...

New page

'''Unreleased structure'''

The entry 5cmg is ON HOLD

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

Description: GTA mutant with mercury-E303C
[[Category: Unreleased Structures]]
[[Category: Gagnon, S.M]]
[[Category: Blackler, R.J]]