2bcm
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(New page: 200px<br /><applet load="2bcm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bcm, resolution 1.480Å" /> '''DaaE adhesin'''<br ...)
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Revision as of 06:36, 21 November 2007
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DaaE adhesin
Overview
DaaE is a member of the Dr adhesin family of Escherichia coli, members of, which are associated with diarrhea and urinary tract infections. A, receptor for Dr adhesins is the cell surface protein, decay-accelerating, factor (DAF). We have carried out a functional analysis of Dr adhesins, as, well as mutagenesis and crystallographic studies of DaaE, to obtain, detailed molecular information about interactions of Dr adhesins with, their receptors. The crystal structure of DaaE has been solved at 1.48 A, resolution. Trimers of the protein are found in the crystal, as has been, the case for other Dr adhesins. Naturally occurring variants and directed, mutations in DaaE have been generated and analyzed for their ability to, bind DAF. Mapping of the mutation sites onto the DaaE molecular structure, shows that several of them contribute to a contiguous surface that is, likely the primary DAF-binding site. The DAF-binding properties of, purified fimbriae and adhesin proteins from mutants and variants, correlated with the ability of bacteria expressing these proteins to bind, to human epithelial cells in culture. DaaE, DraE, AfaE-III, and AfaE-V, interact with complement control protein (CCP) domains 2-4 of DAF, and, analysis of the ionic strength dependence of their binding indicates that, the intermolecular interactions are highly electrostatic in nature. The, adhesins AfaE-I and NfaE-2 bind to CCP-3 and CCP-4 of DAF, and, electrostatic interactions contribute significantly less to these, interactions. These observations are consistent with structural, predictions for these Dr variants and also suggest a role for the, positively charged region linking CCP-2 and CCP-3 of DAF in electrostatic, Dr adhesin-DAF interactions.
About this Structure
2BCM is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure and mutational analysis of the DaaE adhesin of Escherichia coli., Korotkova N, Le Trong I, Samudrala R, Korotkov K, Van Loy CP, Bui AL, Moseley SL, Stenkamp RE, J Biol Chem. 2006 Aug 4;281(31):22367-77. Epub 2006 Jun 2. PMID:16751628
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