In this section
@article{Lee:2016:10.1002/pro.2982,
author = {Lee, W-C and Matthews, S and Garnett, JA},
doi = {10.1002/pro.2982},
journal = {Protein Science},
pages = {1898--1905},
title = {Crystal structure and analysis of HdaB: the Enteroaggregative Escherichia coli AAF/IV pilus tip protein},
url = {http://dx.doi.org/10.1002/pro.2982},
volume = {25},
year = {2016}
}
TY - JOUR
AB - Enteroaggregative Escherichia coli is the primary cause of pediatric diarrhea indeveloping countries and utilize aggregative adherence fimbriae (AAFs) to promoteinitial adherence to the host intestinal mucosa, promote the formation of biofilms andmediate host invasion. Five AAFs have been identified to date and AAF/IV is amongstthe most prevalent found in clinical isolates. Here we present the X-ray crystal structureof the AAF/IV tip protein HdaB at 2.0 Å resolution. It shares high structural homologywith members of the Afa/Dr superfamily of fimbriae, which are involved in hostinvasion. We highlight surface exposed residues that share sequence homology andpropose that these may function in invasion and also non-conserved regions that couldmediate HdaB specific adhesive functions.
AU - Lee,W-C
AU - Matthews,S
AU - Garnett,JA
DO - 10.1002/pro.2982
EP - 1905
PY - 2016///
SN - 1469-896X
SP - 1898
TI - Crystal structure and analysis of HdaB: the Enteroaggregative Escherichia coli AAF/IV pilus tip protein
T2 - Protein Science
UR - http://dx.doi.org/10.1002/pro.2982
UR - http://hdl.handle.net/10044/1/34752
VL - 25
ER -
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