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2ixq
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:2ixq.png|left|200px]] | ||
| - | + | ==The solution structure of the invasive tip complex from Afa-Dr fibrils== | |
| - | + | <StructureSection load='2ixq' size='340' side='right'caption='[[2ixq]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2ixq]] is a 2 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=2IXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IXQ 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;'>[[1rxl|1rxl]], [[1usz|1usz]], [[1ut2|1ut2]]</div></td></tr> | |
| - | - | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">afaD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), afaE3, afaE-3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=2ixq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ixq OCA], [https://pdbe.org/2ixq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ixq RCSB], [https://www.ebi.ac.uk/pdbsum/2ixq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ixq ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/AFAE3_ECOLX AFAE3_ECOLX]] Hemagglutinins of uropathogenic E.coli mediate adherence to the upper urinary tract. These adhesins bind to the Dr blood group antigen and also agglutinate human erythrocytes in the presence of D-mannose (mannose-resistant hemagglutination (MRHA)). | ||
| + | == 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/ix/2ixq_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2ixq 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2ixq" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | --> | + | <references/> |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Bacillus coli migula 1895]] |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Altroff, H]] | |
| - | + | [[Category: Anderson, K L]] | |
| - | + | [[Category: Bouguenec, C Le]] | |
| - | [[Category: | + | [[Category: Cota, E]] |
| - | [[Category: Altroff, H | + | [[Category: Guignot, J]] |
| - | [[Category: Anderson, K L | + | [[Category: Jones, C]] |
| - | [[Category: Bouguenec, C Le | + | [[Category: Mardon, H]] |
| - | [[Category: Cota, E | + | [[Category: Matthews, S]] |
| - | [[Category: Guignot, J | + | [[Category: Merle, L du]] |
| - | [[Category: Jones, C | + | [[Category: Servin, A]] |
| - | [[Category: Mardon, H | + | [[Category: Simpson, P]] |
| - | [[Category: Matthews, S | + | |
| - | [[Category: Merle, L | + | |
| - | [[Category: Servin, A | + | |
| - | [[Category: Simpson, P | + | |
[[Category: Afae]] | [[Category: Afae]] | ||
[[Category: Afimbrial sheath]] | [[Category: Afimbrial sheath]] | ||
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[[Category: Structural protein]] | [[Category: Structural protein]] | ||
[[Category: Upec]] | [[Category: Upec]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:36:45 2008'' | ||
Current revision
The solution structure of the invasive tip complex from Afa-Dr fibrils
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Categories: Bacillus coli migula 1895 | Large Structures | Altroff, H | Anderson, K L | Bouguenec, C Le | Cota, E | Guignot, J | Jones, C | Mardon, H | Matthews, S | Merle, L du | Servin, A | Simpson, P | Afae | Afimbrial sheath | Cell adhesion | Daec | Daf | Donor strand complemented | Fimbria | Ig-like domain | Structural protein | Upec

