8gn6
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystallization of Sialidase from Porphyromonas gingivalis== | |
| + | <StructureSection load='8gn6' size='340' side='right'caption='[[8gn6]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8gn6]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Porphyromonas_gingivalis Porphyromonas gingivalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GN6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GN6 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</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=8gn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gn6 OCA], [https://pdbe.org/8gn6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gn6 RCSB], [https://www.ebi.ac.uk/pdbsum/8gn6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gn6 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A1R4DV85_PORGN A0A1R4DV85_PORGN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The sialidases, which catalyze the hydrolysis of sialic acid from extracellular glycoconjugates, are a group of major virulence factors in various pathogenic bacteria. In Porphyromonas gingivalis, which causes human periodontal disease, sialidase contributes to bacterial pathogenesis via promoting the formation of biofilms and capsules, reducing the ability for macrophage clearance, and providing nutrients for bacterial colonization. Here, the crystal structure of the P. gingivalis sialidase SiaPG is reported at 2.1 A resolution, revealing an N-terminal carbohydrate-binding domain followed by a canonical C-terminal catalytic domain. Simulation of the product sialic acid in the active-site pocket together with functional analysis enables clear identification of the key residues that are required for substrate binding and catalysis. Moreover, structural comparison with other sialidases reveals distinct features of the active-site pocket which might confer substrate specificity. These findings provide the structural basis for the further design and optimization of effective inhibitors to target SiaPG to fight against P. gingivalis-derived oral diseases. | ||
| - | + | Structural and enzymatic characterization of the sialidase SiaPG from Porphyromonas gingivalis.,Dong WB, Jiang YL, Zhu ZL, Zhu J, Li Y, Xia R, Zhou K Acta Crystallogr F Struct Biol Commun. 2023 Apr 1;79(Pt 4):87-94. doi: , 10.1107/S2053230X23001735. Epub 2023 Mar 30. PMID:36995120<ref>PMID:36995120</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Dong | + | <div class="pdbe-citations 8gn6" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Porphyromonas gingivalis]] | ||
| + | [[Category: Dong WB]] | ||
Revision as of 09:28, 19 April 2023
Crystallization of Sialidase from Porphyromonas gingivalis
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