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==Solution structure of the engineered protein Afae-dsc== | |||
<StructureSection load='1rxl' size='340' side='right'caption='[[1rxl]]' scene=''> | |||
| | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1rxl]] 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=1RXL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RXL FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 15 models</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=1rxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rxl OCA], [https://pdbe.org/1rxl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rxl RCSB], [https://www.ebi.ac.uk/pdbsum/1rxl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rxl 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/rx/1rxl_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=1rxl ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Pathogenic bacteria possess adhesion protein complexes that play essential roles in targeting host cells and in propagating infection. Although each family of adhesion proteins is generally associated with a specific human disease, the Dr family from Escherichia coli is a notable exception, as its members are associated with both diarrheal and urinary tract infections. These proteins are reported to form both fimbrial and afimbrial structures at the bacterial cell surface and target a common host cell receptor, the decay-accelerating factor (DAF or CD55). Using the newly solved three-dimensional structure of AfaE, we have constructed a robust atomic resolution model that reveals the structural basis for assembly by donor strand complementation and for the architecture of capped surface fibers. | Pathogenic bacteria possess adhesion protein complexes that play essential roles in targeting host cells and in propagating infection. Although each family of adhesion proteins is generally associated with a specific human disease, the Dr family from Escherichia coli is a notable exception, as its members are associated with both diarrheal and urinary tract infections. These proteins are reported to form both fimbrial and afimbrial structures at the bacterial cell surface and target a common host cell receptor, the decay-accelerating factor (DAF or CD55). Using the newly solved three-dimensional structure of AfaE, we have constructed a robust atomic resolution model that reveals the structural basis for assembly by donor strand complementation and for the architecture of capped surface fibers. | ||
An atomic resolution model for assembly, architecture, and function of the Dr adhesins.,Anderson KL, Billington J, Pettigrew D, Cota E, Simpson P, Roversi P, Chen HA, Urvil P, du Merle L, Barlow PN, Medof ME, Smith RA, Nowicki B, Le Bouguenec C, Lea SM, Matthews S Mol Cell. 2004 Aug 27;15(4):647-57. PMID:15327779<ref>PMID:15327779</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1rxl" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Anderson | [[Category: Anderson KL]] | ||
[[Category: Barlow | [[Category: Barlow PN]] | ||
[[Category: Billington | [[Category: Billington J]] | ||
[[Category: | [[Category: Chen HA]] | ||
[[Category: | [[Category: Cota E]] | ||
[[Category: | [[Category: Le Bouguenec C]] | ||
[[Category: Lea | [[Category: Lea SM]] | ||
[[Category: Matthews | [[Category: Matthews S]] | ||
[[Category: Medof | [[Category: Medof ME]] | ||
[[Category: Nowicki B]] | |||
[[Category: Nowicki | [[Category: Pettigrew D]] | ||
[[Category: Pettigrew | [[Category: Roversi P]] | ||
[[Category: Roversi | [[Category: Simpson P]] | ||
[[Category: Simpson | [[Category: Smith RA]] | ||
[[Category: Smith | [[Category: Urvil P]] | ||
[[Category: Urvil | [[Category: Du Merle L]] | ||
[[Category: | |||
Latest revision as of 11:47, 6 November 2024
Solution structure of the engineered protein Afae-dscSolution structure of the engineered protein Afae-dsc
Structural highlights
FunctionAFAE3_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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPathogenic bacteria possess adhesion protein complexes that play essential roles in targeting host cells and in propagating infection. Although each family of adhesion proteins is generally associated with a specific human disease, the Dr family from Escherichia coli is a notable exception, as its members are associated with both diarrheal and urinary tract infections. These proteins are reported to form both fimbrial and afimbrial structures at the bacterial cell surface and target a common host cell receptor, the decay-accelerating factor (DAF or CD55). Using the newly solved three-dimensional structure of AfaE, we have constructed a robust atomic resolution model that reveals the structural basis for assembly by donor strand complementation and for the architecture of capped surface fibers. An atomic resolution model for assembly, architecture, and function of the Dr adhesins.,Anderson KL, Billington J, Pettigrew D, Cota E, Simpson P, Roversi P, Chen HA, Urvil P, du Merle L, Barlow PN, Medof ME, Smith RA, Nowicki B, Le Bouguenec C, Lea SM, Matthews S Mol Cell. 2004 Aug 27;15(4):647-57. PMID:15327779[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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