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3crf

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==Electron Microscopy model of the Saf Pilus- Type B==
==Electron Microscopy model of the Saf Pilus- Type B==
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<StructureSection load='3crf' size='340' side='right' caption='[[3crf]], [[Resolution|resolution]] 17.00&Aring;' scene=''>
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<SX load='3crf' size='340' side='right' viewer='molstar' caption='[[3crf]], [[Resolution|resolution]] 17.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3crf]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CRF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CRF FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3crf]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CRF FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2co4|2co4]], [[3cre|3cre]]</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">Electron Microscopy, [[Resolution|Resolution]] 17&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">safA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 Salmonella enterica subsp. enterica serovar Typhimurium])</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=3crf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3crf OCA], [https://pdbe.org/3crf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3crf RCSB], [https://www.ebi.ac.uk/pdbsum/3crf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3crf ProSAT]</span></td></tr>
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<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=3crf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3crf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3crf RCSB], [http://www.ebi.ac.uk/pdbsum/3crf PDBsum]</span></td></tr>
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</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/Q8ZRK4_SALTY Q8ZRK4_SALTY]
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Bacterial pili are important virulence factors involved in host cell attachment and/or biofilm formation, key steps in establishing and maintaining successful infection. Here we studied Salmonella atypical fimbriae (or Saf pili), formed by the conserved chaperone/usher pathway. In contrast to the well-established quaternary structure of typical/FGS-chaperone assembled, rod-shaped, chaperone/usher pili, little is known about the supramolecular organisation in atypical/FGL-chaperone assembled fimbriae. In our study, we have used negative stain electron microscopy and single-particle image analysis to determine the three-dimensional structure of the Salmonella typhimurium Saf pilus. Our results show atypical/FGL-chaperone assembled fimbriae are composed of highly flexible linear multi-subunit fibres that are formed by globular subunits connected to each other by short links giving a "beads on a string"-like appearance. Quantitative fitting of the atomic structure of the SafA pilus subunit into the electron density maps, in combination with linker modelling and energy minimisation, has enabled analysis of subunit arrangement and intersubunit interactions in the Saf pilus. Short intersubunit linker regions provide the molecular basis for flexibility of the Saf pilus by acting as molecular hinges allowing a large range of movement between consecutive subunits in the fibre.
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Structural analysis of the Saf pilus by electron microscopy and image processing.,Salih O, Remaut H, Waksman G, Orlova EV J Mol Biol. 2008 May 23;379(1):174-87. Epub 2008 Apr 3. PMID:18448124<ref>PMID:18448124</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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== References ==
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<references/>
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__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
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[[Category: Large Structures]]
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[[Category: Orlova, E V]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]]
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[[Category: Remaut, H]]
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[[Category: Orlova EV]]
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[[Category: Salih, O]]
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[[Category: Remaut H]]
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[[Category: Waksman, G]]
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[[Category: Salih O]]
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[[Category: Fibril protein]]
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[[Category: Waksman G]]
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[[Category: Membrane protein]]
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[[Category: Safa protein polymer]]
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[[Category: Type b saf pilus]]
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Current revision

Electron Microscopy model of the Saf Pilus- Type B

3crf, resolution 17.00Å

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