Structural highlights
Function
B3V224_ECOLX Q08JP6_ECOLX
Publication Abstract from PubMed
Enteroaggregative Escherichia coli is the primary cause of pediatric diarrhea in developing countries. They utilize aggregative adherence fimbriae (AAFs) to promote initial adherence to the host intestinal mucosa, promote the formation of biofilms, and mediate host invasion. Five AAFs have been identified to date and AAF/IV is amongst the most prevalent found in clinical isolates. Here we present the X-ray crystal structure of the AAF/IV tip protein HdaB at 2.0 A resolution. It shares high structural homology with members of the Afa/Dr superfamily of fimbriae, which are involved in host invasion. We highlight surface exposed residues that share sequence homology and propose that these may function in invasion and also non-conserved regions that could mediate HdaB specific adhesive functions.
Crystal structure and analysis of HdaB: The enteroaggregative Escherichia coli AAF/IV pilus tip protein.,Lee WC, Matthews S, Garnett JA Protein Sci. 2016 Jul 12. doi: 10.1002/pro.2982. PMID:27400770[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lee WC, Matthews S, Garnett JA. Crystal structure and analysis of HdaB: The enteroaggregative Escherichia coli AAF/IV pilus tip protein. Protein Sci. 2016 Jul 12. doi: 10.1002/pro.2982. PMID:27400770 doi:http://dx.doi.org/10.1002/pro.2982