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2fvn

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(New page: 200px<br /><applet load="2fvn" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fvn" /> '''The fibrillar tip complex of the Afa/Dr adhe...)
Current revision (14:37, 29 December 2021) (edit) (undo)
 
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[[Image:2fvn.jpg|left|200px]]<br /><applet load="2fvn" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2fvn" />
 
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'''The fibrillar tip complex of the Afa/Dr adhesins from pathogen E. coli displays synergistic binding to 5 1 and v 3 integrins'''<br />
 
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==Overview==
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==The fibrillar tip complex of the Afa/Dr adhesins from pathogen E. coli displays synergistic binding to 5 1 and v 3 integrins==
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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.
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<StructureSection load='2fvn' size='340' side='right'caption='[[2fvn]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2fvn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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>
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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;'>[[1rxl|1rxl]]</div></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=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>
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</table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fv/2fvn_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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2FVN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FVN OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16965519 16965519]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 2fvn" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Anderson, K.L.]]
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<references/>
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[[Category: Cota, E.]]
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__TOC__
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[[Category: Matthews, S.J.]]
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</StructureSection>
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[[Category: Simpson, P.]]
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[[Category: Bacillus coli migula 1895]]
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[[Category: afad]]
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[[Category: Large Structures]]
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[[Category: afae]]
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[[Category: Anderson, K L]]
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[[Category: afimbrial]]
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[[Category: Cota, E]]
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[[Category: ceacam]]
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[[Category: Matthews, S J]]
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[[Category: daec]]
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[[Category: Simpson, P]]
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[[Category: daf]]
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[[Category: Afad]]
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[[Category: fibrillar]]
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[[Category: Afae]]
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[[Category: integrin-binding]]
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[[Category: Afimbrial]]
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[[Category: Ceacam]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:47:42 2007''
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[[Category: Cell adhesion]]
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[[Category: Daec]]
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[[Category: Daf]]
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[[Category: Fibrillar]]
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[[Category: Integrin-binding]]

Current revision

The fibrillar tip complex of the Afa/Dr adhesins from pathogen E. coli displays synergistic binding to 5 1 and v 3 integrins

PDB ID 2fvn

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