2wle - Revision history

OCA at 07:10, 1 May 2024

OCA — Wed, 01 May 2024 07:10:20 GMT

←Older revision		Revision as of 07:10, 1 May 2024
Line 3:		Line 3:
	<StructureSection load='2wle' size='340' side='right'caption='[[2wle]], [[Resolution\|resolution]] 2.19Å' scene=''>		<StructureSection load='2wle' size='340' side='right'caption='[[2wle]], [[Resolution\|resolution]] 2.19Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2wle]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Neisseria_meningitidis_serogroup_y~~ Neisseria meningitidis serogroup y]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WLE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WLE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2wle]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_Y Neisseria meningitidis serogroup Y]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WLE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WLE FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 2.19Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2wlc\|2wlc]], [[2wld\|2wld]], [[2wlf\|2wlf]], [[2wlg\|2wlg]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=2wle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wle OCA], [https://pdbe.org/2wle PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wle RCSB], [https://www.ebi.ac.uk/pdbsum/2wle PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wle 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=2wle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wle OCA], [https://pdbe.org/2wle PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wle RCSB], [https://www.ebi.ac.uk/pdbsum/2wle PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wle ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/OATWY_NEIME OATWY_NEIME] Catalyzes the O-acetylation of capsular polymeric sialic acid consisting of polymers of (2->6)-alpha-D-glucosyl-(1->4)-N-acetyl-alpha-D-neuraminosyl residues. Shows high substrate specificity toward polymers of sialic acid that contains a large number of residues.<ref>PMID:19525232</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 18:		Line 20:
	</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=2wle 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=2wle ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The neuroinvasive pathogen Neisseria meningitidis has 13 capsular serogroups, but the majority of disease is caused by only 5 of these. Groups B, C, Y, and W-135 all display a polymeric sialic acid-containing capsule that provides a means for the bacteria to evade the immune response during infection by mimicking host sialic acid-containing cell surface structures. These capsules in serogroups C, Y, and W-135 can be further acetylated by a sialic acid-specific O-acetyltransferase, a modification that correlates with decreased immunoreactivity and increased virulence. In N. meningitidis serogroup Y, the O-acetylation reaction is catalyzed by the enzyme OatWY, which we show has clear specificity toward the serogroup Y capsule ([Glc-(alpha1-->4)-Sia](n)). To understand the underlying molecular basis of this process, we have performed crystallographic analysis of OatWY with bound substrate as well as determined kinetic parameters of the wild type enzyme and active site mutants. The structure of OatWY reveals an intimate homotrimer of left-handed beta-helix motifs that frame a deep active site cleft selective for the polysialic acid-bearing substrate. Within the active site, our structural, kinetic, and mutagenesis data support the role of two conserved residues in the catalytic mechanism (His-121 and Trp-145) and further highlight a significant movement of Tyr-171 that blocks the active site of the enzyme in its native form. Collectively, our results reveal the first structural features of a bacterial sialic acid O-acetyltransferase and provide significant new insight into its catalytic mechanism and specificity for the capsular polysaccharide of serogroup Y meningococci.
-
-	Structural and kinetic characterizations of the polysialic acid O-acetyltransferase OatWY from Neisseria meningitidis.,Lee HJ, Rakic B, Gilbert M, Wakarchuk WW, Withers SG, Strynadka NC J Biol Chem. 2009 Sep 4;284(36):24501-11. Epub 2009 Jun 12. PMID:19525232<ref>PMID:19525232</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2wle" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Neisseria meningitidis serogroup y]]	+	[[Category: Neisseria meningitidis serogroup Y]]
-	[[Category: Gilbert, M]]	+	[[Category: Gilbert M]]
-	[[Category: Lee~~, H J~~]]	+	[[Category: Lee HJ]]
-	[[Category: Rakic, B]]	+	[[Category: Rakic B]]
-	[[Category: Strynadka~~, N C.J~~]]	+	[[Category: Strynadka NCJ]]
-	[[Category: Wakarchuk~~, W W~~]]	+	[[Category: Wakarchuk WW]]
-	[[Category: Withers~~, S G]]~~	+	[[Category: Withers SG]]
-	~~[[Category: Acetyltransferase]]~~	+
-	~~[[Category: Enzyme]]~~	+
-	~~[[Category: Left-handed beta helix]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 11:10, 6 April 2022

OCA — Wed, 06 Apr 2022 11:10:14 GMT

←Older revision		Revision as of 11:10, 6 April 2022
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	<StructureSection load='2wle' size='340' side='right'caption='[[2wle]], [[Resolution\|resolution]] 2.19Å' scene=''>		<StructureSection load='2wle' size='340' side='right'caption='[[2wle]], [[Resolution\|resolution]] 2.19Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2wle]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_y Neisseria meningitidis serogroup y]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WLE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2WLE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2wle]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_y Neisseria meningitidis serogroup y]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WLE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WLE FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wlc\|2wlc]], [[2wld\|2wld]], [[2wlf\|2wlf]], [[2wlg\|2wlg]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2wlc\|2wlc]], [[2wld\|2wld]], [[2wlf\|2wlf]], [[2wlg\|2wlg]]</div></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=2wle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wle OCA], [~~http~~://pdbe.org/2wle PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2wle RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2wle PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2wle 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=2wle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wle OCA], [https://pdbe.org/2wle PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wle RCSB], [https://www.ebi.ac.uk/pdbsum/2wle PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wle ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==

OCA at 08:53, 1 July 2020

OCA — Wed, 01 Jul 2020 08:53:21 GMT

←Older revision		Revision as of 08:53, 1 July 2020
Line 1:		Line 1:

	==Crystallographic analysis of the polysialic acid O-acetyltransferase OatWY==		==Crystallographic analysis of the polysialic acid O-acetyltransferase OatWY==
-	<StructureSection load='2wle' size='340' side='right' caption='[[2wle]], [[Resolution\|resolution]] 2.19Å' scene=''>	+	<StructureSection load='2wle' size='340' side='right'caption='[[2wle]], [[Resolution\|resolution]] 2.19Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2wle]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_y Neisseria meningitidis serogroup y]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WLE OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2WLE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2wle]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_y Neisseria meningitidis serogroup y]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WLE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2WLE FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wlc\|2wlc]], [[2wld\|2wld]], [[2wlf\|2wlf]], [[2wlg\|2wlg]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wlc\|2wlc]], [[2wld\|2wld]], [[2wlf\|2wlf]], [[2wlg\|2wlg]]</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=2wle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wle OCA], [http://pdbe.org/2wle PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wle RCSB], [http://www.ebi.ac.uk/pdbsum/2wle PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wle ProSAT]</span></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=2wle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wle OCA], [http://pdbe.org/2wle PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wle RCSB], [http://www.ebi.ac.uk/pdbsum/2wle PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wle ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Neisseria meningitidis serogroup y]]		[[Category: Neisseria meningitidis serogroup y]]
	[[Category: Gilbert, M]]		[[Category: Gilbert, M]]

OCA at 09:06, 26 September 2018

OCA — Wed, 26 Sep 2018 09:06:02 GMT

←Older revision		Revision as of 09:06, 26 September 2018
Line 1:		Line 1:
-	==~~CRYSTALLOGRAPHIC ANALYSIS OF THE POLYSIALIC ACID~~ O-~~ACETYLTRANSFERASE OATWY~~==	+
		+	==Crystallographic analysis of the polysialic acid O-acetyltransferase OatWY==
	<StructureSection load='2wle' size='340' side='right' caption='[[2wle]], [[Resolution\|resolution]] 2.19Å' scene=''>		<StructureSection load='2wle' size='340' side='right' caption='[[2wle]], [[Resolution\|resolution]] 2.19Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wlc\|2wlc]], [[2wld\|2wld]], [[2wlf\|2wlf]], [[2wlg\|2wlg]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wlc\|2wlc]], [[2wld\|2wld]], [[2wlf\|2wlf]], [[2wlg\|2wlg]]</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=2wle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wle OCA], [http://pdbe.org/2wle PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wle RCSB], [http://www.ebi.ac.uk/pdbsum/2wle 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=2wle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wle OCA], [http://pdbe.org/2wle PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wle RCSB], [http://www.ebi.ac.uk/pdbsum/2wle PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wle ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 11:		Line 12:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wl/2wle_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wl/2wle_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 02:31, 9 February 2016

OCA — Tue, 09 Feb 2016 02:31:29 GMT

←Older revision		Revision as of 02:31, 9 February 2016
Line 5:		Line 5:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wlc\|2wlc]], [[2wld\|2wld]], [[2wlf\|2wlf]], [[2wlg\|2wlg]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wlc\|2wlc]], [[2wld\|2wld]], [[2wlf\|2wlf]], [[2wlg\|2wlg]]</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=2wle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wle OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wle RCSB], [http://www.ebi.ac.uk/pdbsum/2wle 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=2wle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wle OCA], [http://pdbe.org/2wle PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wle RCSB], [http://www.ebi.ac.uk/pdbsum/2wle PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 15:		Line 15:
	<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=2wle ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 25:		Line 25:
	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 2wle" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:11, 20 January 2015

OCA — Tue, 20 Jan 2015 10:11:49 GMT

←Older revision		Revision as of 10:11, 20 January 2015
Line 30:		Line 30:
	</StructureSection>		</StructureSection>
	[[Category: Neisseria meningitidis serogroup y]]		[[Category: Neisseria meningitidis serogroup y]]
-	[[Category: Gilbert, M.]]	+	[[Category: Gilbert, M]]
-	[[Category: Lee, H J.]]	+	[[Category: Lee, H J]]
-	[[Category: Rakic, B.]]	+	[[Category: Rakic, B]]
-	[[Category: Strynadka, N C.J.]]	+	[[Category: Strynadka, N C.J]]
-	[[Category: Wakarchuk, W W.]]	+	[[Category: Wakarchuk, W W]]
-	[[Category: Withers, S G.]]	+	[[Category: Withers, S G]]
	[[Category: Acetyltransferase]]		[[Category: Acetyltransferase]]
	[[Category: Enzyme]]		[[Category: Enzyme]]
	[[Category: Left-handed beta helix]]		[[Category: Left-handed beta helix]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 05:56, 10 October 2014

OCA — Fri, 10 Oct 2014 05:56:54 GMT

←Older revision		Revision as of 05:56, 10 October 2014
Line 2:		Line 2:
	<StructureSection load='2wle' size='340' side='right' caption='[[2wle]], [[Resolution\|resolution]] 2.19Å' scene=''>		<StructureSection load='2wle' size='340' side='right' caption='[[2wle]], [[Resolution\|resolution]] 2.19Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2wle]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_y Neisseria meningitidis serogroup y]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WLE OCA]. <br>	+	<table><tr><td colspan='2'>[[2wle]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_y Neisseria meningitidis serogroup y]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WLE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WLE FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wlc\|2wlc]], [[2wld\|2wld]], [[2wlf\|2wlf]], [[2wlg\|2wlg]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wlc\|2wlc]], [[2wld\|2wld]], [[2wlf\|2wlf]], [[2wlg\|2wlg]]</td></tr>
-	<tr~~><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class~~='~~plainlinks~~'~~>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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=2wle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wle OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wle RCSB], [http://www.ebi.ac.uk/pdbsum/2wle PDBsum]</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=2wle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wle OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wle RCSB], [http://www.ebi.ac.uk/pdbsum/2wle PDBsum]</span></td></tr>	+	</table>
-	<table>	+
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	Structural and kinetic characterizations of the polysialic acid O-acetyltransferase OatWY from Neisseria meningitidis.,Lee HJ, Rakic B, Gilbert M, Wakarchuk WW, Withers SG, Strynadka NC J Biol Chem. 2009 Sep 4;284(36):24501-11. Epub 2009 Jun 12. PMID:19525232<ref>PMID:19525232</ref>		Structural and kinetic characterizations of the polysialic acid O-acetyltransferase OatWY from Neisseria meningitidis.,Lee HJ, Rakic B, Gilbert M, Wakarchuk WW, Withers SG, Strynadka NC J Biol Chem. 2009 Sep 4;284(36):24501-11. Epub 2009 Jun 12. PMID:19525232<ref>PMID:19525232</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>
	== References ==		== References ==

OCA at 08:38, 7 May 2014

OCA — Wed, 07 May 2014 08:38:55 GMT

←Older revision		Revision as of 08:38, 7 May 2014
Line 1:		Line 1:
-	[[~~Image:~~2wle.~~png~~\|~~left~~\|200px]]	+	==CRYSTALLOGRAPHIC ANALYSIS OF THE POLYSIALIC ACID O-ACETYLTRANSFERASE OATWY==
		+	<StructureSection load='2wle' size='340' side='right' caption='[[2wle]], [[Resolution\|resolution]] 2.19Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2wle]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_y Neisseria meningitidis serogroup y]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WLE OCA]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2wlc\|2wlc]], [[2wld\|2wld]], [[2wlf\|2wlf]], [[2wlg\|2wlg]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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=2wle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wle OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wle RCSB], [http://www.ebi.ac.uk/pdbsum/2wle 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/wl/2wle_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 neuroinvasive pathogen Neisseria meningitidis has 13 capsular serogroups, but the majority of disease is caused by only 5 of these. Groups B, C, Y, and W-135 all display a polymeric sialic acid-containing capsule that provides a means for the bacteria to evade the immune response during infection by mimicking host sialic acid-containing cell surface structures. These capsules in serogroups C, Y, and W-135 can be further acetylated by a sialic acid-specific O-acetyltransferase, a modification that correlates with decreased immunoreactivity and increased virulence. In N. meningitidis serogroup Y, the O-acetylation reaction is catalyzed by the enzyme OatWY, which we show has clear specificity toward the serogroup Y capsule ([Glc-(alpha1-->4)-Sia](n)). To understand the underlying molecular basis of this process, we have performed crystallographic analysis of OatWY with bound substrate as well as determined kinetic parameters of the wild type enzyme and active site mutants. The structure of OatWY reveals an intimate homotrimer of left-handed beta-helix motifs that frame a deep active site cleft selective for the polysialic acid-bearing substrate. Within the active site, our structural, kinetic, and mutagenesis data support the role of two conserved residues in the catalytic mechanism (His-121 and Trp-145) and further highlight a significant movement of Tyr-171 that blocks the active site of the enzyme in its native form. Collectively, our results reveal the first structural features of a bacterial sialic acid O-acetyltransferase and provide significant new insight into its catalytic mechanism and specificity for the capsular polysaccharide of serogroup Y meningococci.

-	<!--	+	Structural and kinetic characterizations of the polysialic acid O-acetyltransferase OatWY from Neisseria meningitidis.,Lee HJ, Rakic B, Gilbert M, Wakarchuk WW, Withers SG, Strynadka NC J Biol Chem. 2009 Sep 4;284(36):24501-11. Epub 2009 Jun 12. PMID:19525232<ref>PMID:19525232</ref>
-	~~The line below this paragraph~~, ~~containing "STRUCTURE_2wle"~~, ~~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_2wle\| PDB=2wle \| SCENE= }}~~	+

-	~~===CRYSTALLOGRAPHIC ANALYSIS OF THE POLYSIALIC ACID O-ACETYLTRANSFERASE OATWY===~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-		+	== References ==
-	~~<!--~~	+	<references/>
-	~~The line below this paragraph~~, ~~{{ABSTRACT_PUBMED_19525232}}, adds~~ the ~~Publication Abstract to the page~~	+	__TOC__
-	~~(as it appears on PubMed at http://www~~.~~pubmed~~.~~gov), where 19525232 is the PubMed ID number~~.	+	</StructureSection>
-	-->	+
-	~~{{ABSTRACT_PUBMED_19525232}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[2wle]] is a 3 chain structure with sequence from [http:~~//en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_y Neisseria meningitidis serogroup y]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WLE OCA].	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:019525232<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Neisseria meningitidis serogroup y]]		[[Category: Neisseria meningitidis serogroup y]]
	[[Category: Gilbert, M.]]		[[Category: Gilbert, M.]]

OCA: Protected "2wle" [edit=sysop:move=sysop]

OCA — Wed, 24 Aug 2011 05:24:40 GMT

Protected "2wle" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:24, 24 August 2011

OCA at 05:24, 24 August 2011

OCA — Wed, 24 Aug 2011 05:24:39 GMT

←Older revision		Revision as of 05:24, 24 August 2011
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2wle.png\|left\|200px]]		[[Image:2wle.png\|left\|200px]]

Line 20:		Line 19:

	==About this Structure==		==About this Structure==
-	~~2WLE~~ is a 3 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_y Neisseria meningitidis serogroup y]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WLE OCA].	+	[[2wle]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_y Neisseria meningitidis serogroup y]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WLE OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19525232~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019525232</ref><references group="xtra"/>
	[[Category: Neisseria meningitidis serogroup y]]		[[Category: Neisseria meningitidis serogroup y]]
	[[Category: Gilbert, M.]]		[[Category: Gilbert, M.]]
Line 35:		Line 34:
	[[Category: Left-handed beta helix]]		[[Category: Left-handed beta helix]]
	[[Category: Transferase]]		[[Category: Transferase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 9 08:23:03 2009''