View source for 2fvn


==The fibrillar tip complex of the Afa/Dr adhesins from pathogen E. coli displays synergistic binding to 5 1 and v 3 integrins==
<StructureSection load='2fvn' size='340' side='right'caption='[[2fvn]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2fvn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FVN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</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=2fvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fvn OCA], [https://pdbe.org/2fvn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fvn RCSB], [https://www.ebi.ac.uk/pdbsum/2fvn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fvn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AFAD_ECOLX AFAD_ECOLX] 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fv/2fvn_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fvn ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Afa/Dr family of adhesins are produced by pathogenic Escherichia coli strains that are especially prevalent in chronic diarrhoeal and recurrent urinary tract infections. Most notably, they are found in up to 50% of cystitis cases in children and 30% of pyelonephritis in pregnant women. Afa/Dr adhesins are capped surface fibrils that mediate recognition of the host and subsequent bacterial internalization. Using the newly solved three-dimensional structure of the minimal invasive complex (AfaDE) combined with biochemical and cellular assays, we reveal the architecture of the fibrillar cap and identify a novel mode of synergistic integrin recognition.

The solution structure of the invasive tip complex from Afa/Dr fibrils.,Cota E, Jones C, Simpson P, Altroff H, Anderson KL, du Merle L, Guignot J, Servin A, Le Bouguenec C, Mardon H, Matthews S Mol Microbiol. 2006 Oct;62(2):356-66. Epub 2006 Sep 8. PMID:16965519<ref>PMID:16965519</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2fvn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Anderson KL]]
[[Category: Cota E]]
[[Category: Matthews SJ]]
[[Category: Simpson P]]