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| | {{STRUCTURE_2bcm| PDB=2bcm | SCENE= }} | | {{STRUCTURE_2bcm| PDB=2bcm | SCENE= }} |
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| - | '''DaaE adhesin'''
| + | ===DaaE adhesin=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16751628}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16751628 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16751628}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Daae adhesin]] | | [[Category: Daae adhesin]] |
| | [[Category: Donor strand complementation]] | | [[Category: Donor strand complementation]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:06:44 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:32:02 2008'' |
Revision as of 05:32, 29 July 2008
Template:STRUCTURE 2bcm
DaaE adhesin
Template:ABSTRACT PUBMED 16751628
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
Page seeded by OCA on Tue Jul 29 08:32:02 2008
