2wlc

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{{Seed}}
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==CRYSTALLOGRAPHIC ANALYSIS OF THE POLYSIALIC ACID O-ACETYLTRANSFERASE OATWY==
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[[Image:2wlc.png|left|200px]]
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<StructureSection load='2wlc' size='340' side='right' caption='[[2wlc]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2wlc]] is a 1 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=2WLC OCA]. <br>
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</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wld|2wld]], [[2wlf|2wlf]], [[2wlg|2wlg]], [[2wle|2wle]]</td></tr>
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<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>
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<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=2wlc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wlc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wlc RCSB], [http://www.ebi.ac.uk/pdbsum/2wlc PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wl/2wlc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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The line below this paragraph, containing "STRUCTURE_2wlc", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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-->
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{{STRUCTURE_2wlc| PDB=2wlc | SCENE= }}
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===CRYSTALLOGRAPHIC ANALYSIS OF THE POLYSIALIC ACID O-ACETYLTRANSFERASE OATWY===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<!--
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_19525232}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 19525232 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_19525232}}
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==About this Structure==
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2WLC is a 1 chain structure of 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=2WLC OCA].
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==Reference==
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<ref group="xtra">PMID:19525232</ref><references group="xtra"/>
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[[Category: Neisseria meningitidis serogroup y]]
[[Category: Neisseria meningitidis serogroup y]]
[[Category: Gilbert, M.]]
[[Category: Gilbert, M.]]
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[[Category: Left-handed beta helix]]
[[Category: Left-handed beta helix]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Aug 4 16:53:42 2009''
 

Revision as of 08:31, 7 May 2014

CRYSTALLOGRAPHIC ANALYSIS OF THE POLYSIALIC ACID O-ACETYLTRANSFERASE OATWY

2wlc, resolution 1.95Å

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