View source for 5lvy


==Structural studies of the Aggregative Adherence Fimbriae of Enteroaggregative Escherichia coli==
<StructureSection load='5lvy' size='340' side='right'caption='[[5lvy]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lvy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O111:H21 Escherichia coli O111:H21]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LVY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LVY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 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=5lvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lvy OCA], [https://pdbe.org/5lvy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lvy RCSB], [https://www.ebi.ac.uk/pdbsum/5lvy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lvy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C9K5V2_ECOLX C9K5V2_ECOLX] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enteroaggregative Escherichia coli (EAEC) is an emerging cause of acute and persistent diarrhea worldwide. The pathogenesis of different EAEC stains is complicated, however, the early essential step begins with attachment of EAEC to intestinal mucosa via aggregative adherence fimbriae (AAFs). Currently, five different variants have been identified, which all share a degree of similarity in the gene organization of their operons and sequences. Here, we report the solution structure of Agg5A from the AAF/V variant. While preserving the major structural features shared by all AAF members, only Agg5A possesses an inserted helix at the beginning of the donor strand, which together with altered surface electrostatics, renders the protein unable to interact with fibronectin. Hence, here we characterize the first AAF variant with a binding mode that varies from previously described AAFs.

Structural and functional studies of Escherichia coli aggregative adherence fimbriae (AAF/V) reveal a deficiency in extracellular matrix binding.,Jonsson R, Liu B, Struve C, Yang Y, Jorgensen R, Xu Y, Jenssen H, Krogfelt KA, Matthews S Biochim Biophys Acta. 2017 Mar;1865(3):304-311. doi:, 10.1016/j.bbapap.2016.11.017. Epub 2016 Dec 9. PMID:27939608<ref>PMID:27939608</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5lvy" style="background-color:#fffaf0;"></div>

==See Also==
*[[Adhesin 3D structures|Adhesin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli O111:H21]]
[[Category: Large Structures]]
[[Category: Liu B]]
[[Category: Matthews S]]