2wld: Difference between revisions

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<StructureSection load='2wld' size='340' side='right'caption='[[2wld]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='2wld' size='340' side='right'caption='[[2wld]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2wld]] 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=2WLD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WLD FirstGlance]. <br>
<table><tr><td colspan='2'>[[2wld]] 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=2WLD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WLD 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=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]] 2.2&#8491;</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]], [[2wlf|2wlf]], [[2wlg|2wlg]], [[2wle|2wle]]</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=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=2wld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wld OCA], [https://pdbe.org/2wld PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wld RCSB], [https://www.ebi.ac.uk/pdbsum/2wld PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wld 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=2wld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wld OCA], [https://pdbe.org/2wld PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wld RCSB], [https://www.ebi.ac.uk/pdbsum/2wld PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wld 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]]
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</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=2wld 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=2wld 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--&gt;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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2wld" 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]]

Latest revision as of 07:10, 1 May 2024

Crystallographic analysis of the polysialic acid O-acetyltransferase OatWY

2wld, resolution 2.20Å

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