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3sok

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Current revision (13:03, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3sok' size='340' side='right'caption='[[3sok]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3sok' size='340' side='right'caption='[[3sok]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3sok]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"fusiformis_nodosus"_beveridge_1941 "fusiformis nodosus" beveridge 1941]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SOK FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3sok]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dichelobacter_nodosus Dichelobacter nodosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SOK FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3soj|3soj]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fimA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=870 "Fusiformis nodosus" Beveridge 1941])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3sok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sok OCA], [https://pdbe.org/3sok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sok RCSB], [https://www.ebi.ac.uk/pdbsum/3sok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sok 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=3sok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sok OCA], [https://pdbe.org/3sok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sok RCSB], [https://www.ebi.ac.uk/pdbsum/3sok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sok ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/FMAA_DICNO FMAA_DICNO]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3sok" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Pilin 3D structures|Pilin 3D structures]]
*[[Pilin 3D structures|Pilin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Fusiformis nodosus beveridge 1941]]
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[[Category: Dichelobacter nodosus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Arvai, A S]]
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[[Category: Arvai AS]]
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[[Category: Craig, L]]
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[[Category: Craig L]]
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[[Category: Hartung, S]]
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[[Category: Hartung S]]
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[[Category: Kolappan, S]]
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[[Category: Kolappan S]]
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[[Category: Shin, D S]]
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[[Category: Shin DS]]
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[[Category: Tainer, J A]]
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[[Category: Tainer JA]]
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[[Category: Wood, T]]
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[[Category: Wood T]]
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[[Category: Cell adhesion]]
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[[Category: Extracellular]]
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[[Category: Pilus subunit]]
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Current revision

Dichelobacter nodosus pilin FimA

PDB ID 3sok

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