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==SeMet AfaE-3 adhesin from Escherichia Coli==
The line below this paragraph, containing "STRUCTURE_1usz", creates the "Structure Box" on the page.
<StructureSection load='1usz' size='340' side='right'caption='[[1usz]], [[Resolution|resolution]] 3.28&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1usz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1USZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1USZ FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.28&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
{{STRUCTURE_1usz| PDB=1usz |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1usz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1usz OCA], [https://pdbe.org/1usz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1usz RCSB], [https://www.ebi.ac.uk/pdbsum/1usz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1usz ProSAT]</span></td></tr>
 
</table>
'''SEMET AFAE-3 ADHESIN FROM ESCHERICHIA COLI'''
== 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 ==
==Overview==
[[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/us/1usz_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=1usz ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pathogenic Escherichia coli expressing Afa/Dr adhesins are able to cause both urinary tract and diarrheal infections. The Afa/Dr adhesins confer adherence to epithelial cells via interactions with the human complement regulating protein, decay accelerating factor (DAF or CD55). Two of the Afa/Dr adhesions, AfaE-III and DraE, differ from each other by only three residues but are reported to have several different properties. One such difference is disruption of the interaction between DraE and CD55 by chloramphenicol, whereas binding of AfaE-III to CD55 is unaffected. Here we present a crystal structure of a strand-swapped trimer of wild type DraE. We also present a crystal structure of this trimer in complex with chloramphenicol, as well as NMR data supporting the binding position of chloramphenicol within the crystal. The crystal structure reveals the precise atomic basis for the sensitivity of DraE-CD55 binding to chloramphenicol and demonstrates that in contrast to other chloramphenicol-protein complexes, drug binding is mediated via recognition of the chlorine "tail" rather than via intercalation of the benzene rings into a hydrophobic pocket.
Pathogenic Escherichia coli expressing Afa/Dr adhesins are able to cause both urinary tract and diarrheal infections. The Afa/Dr adhesins confer adherence to epithelial cells via interactions with the human complement regulating protein, decay accelerating factor (DAF or CD55). Two of the Afa/Dr adhesions, AfaE-III and DraE, differ from each other by only three residues but are reported to have several different properties. One such difference is disruption of the interaction between DraE and CD55 by chloramphenicol, whereas binding of AfaE-III to CD55 is unaffected. Here we present a crystal structure of a strand-swapped trimer of wild type DraE. We also present a crystal structure of this trimer in complex with chloramphenicol, as well as NMR data supporting the binding position of chloramphenicol within the crystal. The crystal structure reveals the precise atomic basis for the sensitivity of DraE-CD55 binding to chloramphenicol and demonstrates that in contrast to other chloramphenicol-protein complexes, drug binding is mediated via recognition of the chlorine "tail" rather than via intercalation of the benzene rings into a hydrophobic pocket.


==About this Structure==
High resolution studies of the Afa/Dr adhesin DraE and its interaction with chloramphenicol.,Pettigrew D, Anderson KL, Billington J, Cota E, Simpson P, Urvil P, Rabuzin F, Roversi P, Nowicki B, du Merle L, Le Bouguenec C, Matthews S, Lea SM J Biol Chem. 2004 Nov 5;279(45):46851-7. Epub 2004 Aug 24. PMID:15331605<ref>PMID:15331605</ref>
1USZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1USZ OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
High resolution studies of the Afa/Dr adhesin DraE and its interaction with chloramphenicol., Pettigrew D, Anderson KL, Billington J, Cota E, Simpson P, Urvil P, Rabuzin F, Roversi P, Nowicki B, du Merle L, Le Bouguenec C, Matthews S, Lea SM, J Biol Chem. 2004 Nov 5;279(45):46851-7. Epub 2004 Aug 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15331605 15331605]
</div>
<div class="pdbe-citations 1usz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Anderson, K L.]]
[[Category: Anderson KL]]
[[Category: Barlow, P.]]
[[Category: Barlow P]]
[[Category: Billington, J.]]
[[Category: Billington J]]
[[Category: Bouguenec, C Le.]]
[[Category: Chen HA]]
[[Category: Chen, H A.]]
[[Category: Cota E]]
[[Category: Cota, E.]]
[[Category: Dumerle L]]
[[Category: Dumerle, L.]]
[[Category: Le Bouguenec C]]
[[Category: Lea, S M.]]
[[Category: Lea SM]]
[[Category: Matthews, S.]]
[[Category: Matthews S]]
[[Category: Medof, E.]]
[[Category: Medof E]]
[[Category: Nowicki, B.]]
[[Category: Nowicki B]]
[[Category: Pettigrew, D.]]
[[Category: Pettigrew D]]
[[Category: Roversi, P.]]
[[Category: Roversi P]]
[[Category: Simpson, P.]]
[[Category: Simpson P]]
[[Category: Smith, R A.G.]]
[[Category: Smith RAG]]
[[Category: Urvil, P.]]
[[Category: Urvil P]]
[[Category: Adhesin]]
[[Category: Afae-3]]
[[Category: Afimbrial adhesin]]
[[Category: Daec]]
[[Category: Upec]]
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