3cre: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(One intermediate revision by the same user not shown)
Line 3: Line 3:
<SX load='3cre' size='340' side='right' viewer='molstar' caption='[[3cre]], [[Resolution|resolution]] 17.00&Aring;' scene=''>
<SX load='3cre' size='340' side='right' viewer='molstar' caption='[[3cre]], [[Resolution|resolution]] 17.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3cre]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CRE FirstGlance]. <br>
<table><tr><td colspan='2'>[[3cre]] 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=3CRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CRE FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2co4|2co4]], [[3crf|3crf]]</div></td></tr>
</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>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">safA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 Salmonella typhimurium])</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=3cre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cre OCA], [https://pdbe.org/3cre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cre RCSB], [https://www.ebi.ac.uk/pdbsum/3cre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cre 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=3cre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cre OCA], [https://pdbe.org/3cre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cre RCSB], [https://www.ebi.ac.uk/pdbsum/3cre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cre ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q8ZRK4_SALTY Q8ZRK4_SALTY]
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.
 
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>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3cre" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</SX>
</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Salmonella typhimurium]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]]
[[Category: Orlova, E V]]
[[Category: Orlova EV]]
[[Category: Remaut, H]]
[[Category: Remaut H]]
[[Category: Salih, O]]
[[Category: Salih O]]
[[Category: Waksman, G]]
[[Category: Waksman G]]
[[Category: Fibril protein]]
[[Category: Membrane protein]]
[[Category: Safa protein polymer]]
[[Category: Type a saf pilus]]

Latest revision as of 09:37, 21 February 2024

Electron Microscopy model of the Saf Pilus- Type A

Loading...

Proteopedia Page Contributors and Editors (what is this?)

OCA