View source for 2ya6


==CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE NANA (TIGR4) IN COMPLEX WITH DANA==
<StructureSection load='2ya6' size='340' side='right' caption='[[2ya6]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ya6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Strpn Strpn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YA6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YA6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DAN:2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC+ACID'>DAN</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ya7|2ya7]], [[2ya4|2ya4]], [[2ya8|2ya8]], [[2ya5|2ya5]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </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=2ya6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ya6 OCA], [http://pdbe.org/2ya6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ya6 RCSB], [http://www.ebi.ac.uk/pdbsum/2ya6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ya6 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The human pathogen Streptococcus pneumoniae is the major cause of bacterial meningitis, respiratory tract infection, septicemia, and otitis media. The bacterium expresses neuraminidase (NA) proteins that contribute to pathogenesis by cleaving sialic acids from host glycoconjugates, thereby enhancing biofilm formation and colonization. Recent in vivo experiments have shown that antiviral compounds, widely used in clinics and designed to inhibit influenza NA, significantly reduce biofilm formation and nasopharyngeal colonization of S. pneumoniae in mice. Here, we present the structural basis for the beneficial effect of these compounds against pneumococcal infection. Crystal structures of pneumococcal NanA in complex with zanamivir and oseltamivir carboxylate are discussed, correlated with measured inhibitory constants K(i), and compared with the binding modes of the inhibitors in the viral enzyme. Inhibitor structures show for the first time how clinically approved anti-influenza compounds interact with an NA of the human pathogen S. pneumoniae and give a rational explanation for their antibacterial effects.

Structural Basis for Streptococcus pneumoniae NanA Inhibition by Influenza Antivirals Zanamivir and Oseltamivir Carboxylate.,Gut H, Xu G, Taylor GL, Walsh MA J Mol Biol. 2011 Jun 17;409(4):496-503. Epub 2011 Apr 14. PMID:21514303<ref>PMID:21514303</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2ya6" style="background-color:#fffaf0;"></div>

==See Also==
*[[Neuraminidase|Neuraminidase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Exo-alpha-sialidase]]
[[Category: Strpn]]
[[Category: Gut, H]]
[[Category: Taylor, G L]]
[[Category: Walsh, M A]]
[[Category: Xu, G]]
[[Category: Hydrolase]]
[[Category: Sialidase]]