2jvu
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(New page: 200px<br /><applet load="2jvu" size="350" color="white" frame="true" align="right" spinBox="true" caption="2jvu" /> '''Solution Structure of Dispersin from Enteroa...)
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Revision as of 06:19, 13 February 2008
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Solution Structure of Dispersin from Enteroaggregative Escherichia coli
Overview
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.
About this Structure
2JVU is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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