3soj: Difference between revisions
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==Francisella tularensis pilin PilE== | |||
<StructureSection load='3soj' size='340' side='right'caption='[[3soj]], [[Resolution|resolution]] 1.00Å' scene=''> | |||
== Structural highlights == | |||
<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='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='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='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> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5NGF6_FRATT Q5NGF6_FRATT] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:22027840</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3soj" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Pilin 3D structures|Pilin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Francisella tularensis subsp. tularensis SCHU S4]] | |||
[[Category: Large Structures]] | |||
[[Category: Arvai AS]] | |||
[[Category: Craig L]] | |||
[[Category: Hartung S]] | |||
[[Category: Kolappan S]] | |||
[[Category: Shin DS]] | |||
[[Category: Tainer JA]] | |||
[[Category: Wood T]] | |||
Latest revision as of 12:41, 30 October 2024
Francisella tularensis pilin PilEFrancisella tularensis pilin PilE
Structural highlights
FunctionPublication Abstract from PubMedPilin 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 AlsoReferences
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