View source for 2jvu


==Solution Structure of Dispersin from Enteroaggregative Escherichia coli==
<StructureSection load='2jvu' size='340' side='right'caption='[[2jvu]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2jvu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_042 Escherichia coli 042]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JVU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JVU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 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=2jvu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jvu OCA], [https://pdbe.org/2jvu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jvu RCSB], [https://www.ebi.ac.uk/pdbsum/2jvu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jvu ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Enteroaggregative Escherichia coli (EAEC), increasingly recognized as an important cause of infant and travelers' diarrhoea, exhibits an aggregative, stacked-brick pattern of adherence to epithelial cells. Adherence is mediated by aggregative adherence fimbriae (AAFs), which are encoded on the pAA virulence plasmid. We recently described a highly prevalent pAA plasmid-borne gene, aap, which encodes a protein (nicknamed dispersin) that is secreted to the bacterial cell surface. Dispersin-null mutants display a unique hyper-aggregating phenotype, accompanied by collapse of AAF pili onto the bacterial cell surface. To study the mechanism of this effect, we solved the structure of dispersin from EAEC strain 042 using solution NMR, revealing a stable beta-sandwich with a conserved net positive surface charge of +3 to +4 among 23 dispersin alleles. Experimental data suggest that dispersin binds non-covalently to lipopolysaccharide on the surface of the bacterium. We also show that the AAF organelles contribute positive charge to the bacterial surface, suggesting that dispersin's role in fimbrial function is to overcome electrostatic attraction between AAF and the bacterial surface.

Solution structure of the novel dispersin protein of enteroaggregative Escherichia coli.,Velarde JJ, Varney KM, Inman KG, Farfan M, Dudley E, Fletcher J, Weber DJ, Nataro JP Mol Microbiol. 2007 Dec;66(5):1123-35. Epub 2007 Nov 6. PMID:17986189<ref>PMID:17986189</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli 042]]
[[Category: Large Structures]]
[[Category: Dudley D]]
[[Category: Farfan K]]
[[Category: Fletcher J]]
[[Category: Inman JG]]
[[Category: Nataro JP]]
[[Category: Varney KM]]
[[Category: Velarde JJ]]
[[Category: Weber DJ]]