4nx9

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Revision as of 08:43, 11 August 2016

Crystal structure of Pseudomonas aeruginosa flagellin FliC

Structural highlights

4nx9 is a 1 chain structure with sequence from "bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:	fliC ("Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Pseudomonas aeruginosa is one of leading opportunistic pathogens in humans and its movement is driven by a flagellar filament that is constituted through the polymerization of a single protein, FliC flagellin (paFliC). paFliC is an essential virulence factor for the colonization of P. aeruginosa. paFliC activates innate immune responses via its recognition by Toll-like receptor 5 (TLR5) and adaptive immunity in the host. Thus, paFliC has been a vaccine candidate to prevent P. aeruginosa infection, particularly for cystic fibrosis patients. To provide structural information on paFliC and its flagellar filament, we have determined the crystal structure of paFliC, which contains the conserved D1 and variable D2 domains, at 2.1A resolution. As observed for Salmonella FliC, the paFliC D1 domain is folded into a rod-shaped structure, and paFliC was demonstrated by gel filtration and native PAGE analyses to directly interact with TLR5. Moreover, a structural model of the paFliC-TLR5 complex suggests that paFliC D1 would provide major TLR5-binding sites, similar to Salmonella FliC. In contrast to the D1 domain, the paFliC D2 domain exhibits a unique structure of two beta-sheets and one alpha-helix that has not been found in other flagellins. An in silico construction of a flagellar filament based on the packing of paFliC in the crystal suggests that the D2 domain would be exposed to solution and could play an important role in immunogenicity. Our biophysical and structure-based modeling study on paFliC, the paFliC-TLR5 complex, and the paFliC filament could contribute to the improvement of vaccine design to control P. aeruginosa infection.

Crystal structure of FliC flagellin from Pseudomonas aeruginosa and its implication in TLR5 binding and formation of the flagellar filament.,Song WS, Yoon SI Biochem Biophys Res Commun. 2014 Jan 14. pii: S0006-291X(14)00023-0. doi:, 10.1016/j.bbrc.2014.01.008. PMID:24434155^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Song WS, Yoon SI. Crystal structure of FliC flagellin from Pseudomonas aeruginosa and its implication in TLR5 binding and formation of the flagellar filament. Biochem Biophys Res Commun. 2014 Jan 14. pii: S0006-291X(14)00023-0. doi:, 10.1016/j.bbrc.2014.01.008. PMID:24434155 doi:http://dx.doi.org/10.1016/j.bbrc.2014.01.008

1 Structural highlights
2 Publication Abstract from PubMed
3 References

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OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4nx9"

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 ==Crystal structure of Pseudomonas aeruginosa flagellin FliC==
 <StructureSection load='4nx9' size='340' side='right' caption='[[4nx9]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fliC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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=4nx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nx9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nx9 RCSB], [http://www.ebi.ac.uk/pdbsum/4nx9 PDBsum]</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=4nx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nx9 OCA], [http://pdbe.org/4nx9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nx9 RCSB], [http://www.ebi.ac.uk/pdbsum/4nx9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nx9 ProSAT]</span></td></tr>
 </table>
 <div style="background-color:#fffaf0;">
@@ Line 15: / Line 16: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4nx9" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4nx9

From Proteopedia

Revision as of 08:43, 11 August 2016

Crystal structure of Pseudomonas aeruginosa flagellin FliC

Structural highlights

Publication Abstract from PubMed

References

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