4yw2: Difference between revisions
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<StructureSection load='4yw2' size='340' side='right'caption='[[4yw2]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='4yw2' size='340' side='right'caption='[[4yw2]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4yw2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4yw2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_TIGR4 Streptococcus pneumoniae TIGR4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YW2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YW2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</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=4yw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yw2 OCA], [https://pdbe.org/4yw2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yw2 RCSB], [https://www.ebi.ac.uk/pdbsum/4yw2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yw2 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=4yw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yw2 OCA], [https://pdbe.org/4yw2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yw2 RCSB], [https://www.ebi.ac.uk/pdbsum/4yw2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yw2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0H2UQE4_STRPN A0A0H2UQE4_STRPN] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Lukacik | [[Category: Streptococcus pneumoniae TIGR4]] | ||
[[Category: Owen | [[Category: Lukacik P]] | ||
[[Category: Potter | [[Category: Owen CD]] | ||
[[Category: Taylor | [[Category: Potter JA]] | ||
[[Category: Walsh | [[Category: Taylor GL]] | ||
[[Category: Walsh M]] | |||
Revision as of 10:28, 10 May 2023
Crystal Structure of Streptococcus pneumoniae NanC, complex 6'SLCrystal Structure of Streptococcus pneumoniae NanC, complex 6'SL
Structural highlights
FunctionPublication Abstract from PubMedStreptococcus pneumoniae is an important human pathogen that causes a range of disease states. Sialidases are important bacterial virulence factors. There are three pneumococcal sialidases: NanA, NanB, and NanC. NanC is an unusual sialidase in that its primary reaction product is 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (Neu5Ac2en, also known as DANA), a nonspecific hydrolytic sialidase inhibitor. The production of Neu5Ac2en from alpha2-3-linked sialosides by the catalytic domain is confirmed within a crystal structure. A covalent complex with 3-fluoro-beta-N-acetylneuraminic acid is also presented, suggesting a common mechanism with other sialidases up to the final step of product formation. A conformation change in an active site hydrophobic loop on ligand binding constricts the entrance to the active site. In addition, the distance between the catalytic acid/base (Asp-315) and the ligand anomeric carbon is unusually short. These features facilitate a novel sialidase reaction in which the final step of product formation is direct abstraction of the C3 proton by the active site aspartic acid, forming Neu5Ac2en. NanC also possesses a carbohydrate-binding module, which is shown to bind alpha2-3- and alpha2-6-linked sialosides, as well as N-acetylneuraminic acid, which is captured in the crystal structure following hydration of Neu5Ac2en by NanC. Overall, the pneumococcal sialidases show remarkable mechanistic diversity while maintaining a common structural scaffold. Streptococcus pneumoniae NanC: STRUCTURAL INSIGHTS INTO THE SPECIFICITY AND MECHANISM OF A SIALIDASE THAT PRODUCES A SIALIDASE INHIBITOR.,Owen CD, Lukacik P, Potter JA, Sleator O, Taylor GL, Walsh MA J Biol Chem. 2015 Nov 13;290(46):27736-48. doi: 10.1074/jbc.M115.673632. Epub, 2015 Sep 14. PMID:26370075[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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