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| | ==Francisella tularensis pilin PilE== | | ==Francisella tularensis pilin PilE== |
| - | <StructureSection load='3soj' size='340' side='right' caption='[[3soj]], [[Resolution|resolution]] 1.00Å' scene=''> | + | <StructureSection load='3soj' size='340' side='right'caption='[[3soj]], [[Resolution|resolution]] 1.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3soj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Fratt Fratt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SOJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SOJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3soj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Francisella_tularensis_subsp._tularensis_SCHU_S4 Francisella tularensis subsp. tularensis SCHU S4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SOJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SOJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sok|3sok]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FTT0889c, FTT_0889c, pilE2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=177416 FRATT])</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=3soj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3soj OCA], [https://pdbe.org/3soj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3soj RCSB], [https://www.ebi.ac.uk/pdbsum/3soj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3soj ProSAT]</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=3soj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3soj OCA], [http://pdbe.org/3soj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3soj RCSB], [http://www.ebi.ac.uk/pdbsum/3soj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3soj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q5NGF6_FRATT Q5NGF6_FRATT] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 3soj" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3soj" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Pilin 3D structures|Pilin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Fratt]] | + | [[Category: Francisella tularensis subsp. tularensis SCHU S4]] |
| - | [[Category: Arvai, A S]] | + | [[Category: Large Structures]] |
| - | [[Category: Craig, L]] | + | [[Category: Arvai AS]] |
| - | [[Category: Hartung, S]] | + | [[Category: Craig L]] |
| - | [[Category: Kolappan, S]] | + | [[Category: Hartung S]] |
| - | [[Category: Shin, D S]] | + | [[Category: Kolappan S]] |
| - | [[Category: Tainer, J A]] | + | [[Category: Shin DS]] |
| - | [[Category: Wood, T]] | + | [[Category: Tainer JA]] |
| - | [[Category: Cell adhesion]]
| + | [[Category: Wood T]] |
| - | [[Category: Extracellular]]
| + | |
| - | [[Category: Pilus subunit]]
| + | |
| Structural highlights
Function
Q5NGF6_FRATT
Publication Abstract from PubMed
Pilin proteins assemble into Type IV pili (T4P), surface-displayed bacterial filaments with virulence functions including motility, attachment, transformation, immune escape, and colony formation. However, challenges in crystallizing full-length fiber-forming and membrane protein pilins leave unanswered questions regarding pilin structures, assembly, functions, and vaccine potential. Here we report pilin structures of full-length DnFimA from the sheep pathogen Dichelobacter nodosus and FtPilE from the human pathogen Francisella tularensis at 2.3 and 1 A resolution, respectively. The DnFimA structure reveals an extended kinked N-terminal alpha-helix, an unusual centrally located disulfide, conserved subdomains, and assembled epitopes informing serogroup vaccines. An interaction between the conserved Glu-5 carboxyl oxygen and the N-terminal amine of an adjacent subunit in the crystallographic dimer is consistent with the hypothesis of a salt bridge between these groups driving T4P assembly. The FtPilE structure identifies an authentic Type IV pilin and provides a framework for understanding the role of T4P in F. tularensis virulence. Combined results define a unified pilin architecture, specialized subdomain roles in pilus assembly and function, and potential therapeutic targets.
Ultrahigh Resolution and Full-length Pilin Structures with Insights for Filament Assembly, Pathogenic Functions, and Vaccine Potential.,Hartung S, Arvai AS, Wood T, Kolappan S, Shin DS, Craig L, Tainer JA J Biol Chem. 2011 Dec 23;286(51):44254-65. Epub 2011 Oct 24. PMID:22027840[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hartung S, Arvai AS, Wood T, Kolappan S, Shin DS, Craig L, Tainer JA. Ultrahigh Resolution and Full-length Pilin Structures with Insights for Filament Assembly, Pathogenic Functions, and Vaccine Potential. J Biol Chem. 2011 Dec 23;286(51):44254-65. Epub 2011 Oct 24. PMID:22027840 doi:10.1074/jbc.M111.297242
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