Citation

BibTex format

@article{Rasheed:2016:10.1016/j.bbapap.2016.07.010,
author = {Rasheed, M and Garnett, J and Perez-Dorado, I and Muhl, D and Filloux, A and Matthews, S},
doi = {10.1016/j.bbapap.2016.07.010},
journal = {Biochimica et Biophysica Acta - Protein Structure},
pages = {1500--1505},
title = {Crystal structure of the CupB6 adhesive tip from the chaperone-usher family of pili from Pseudomonas aeruginosa},
url = {http://dx.doi.org/10.1016/j.bbapap.2016.07.010},
volume = {1864},
year = {2016}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Pseudomonas aeruginosa is a Gram-negative opportunistic bacterial pathogen that can cause chronicinfection of the lungs of cystic fibrosis patients. Chaperone-usher systems in P. aeruginosa are knownto translocate and assemble adhesive pili on the bacterial surface and contribute to biofilm formationwithin the host. Here, we report the crystal structure of the tip adhesion subunit CupB6 from thecupB1-6 gene cluster. The tip domain is connected to the pilus via the N-terminal donor strand fromthe main pilus subunit CupB1. Although the CupB6 adhesion domain bears structural features similarto other CU adhesins it displays an unusual polyproline helix adjacent to a prominent surface pocket,which are likely the site for receptor recognition.
AU  - Rasheed,M
AU  - Garnett,J
AU  - Perez-Dorado,I
AU  - Muhl,D
AU  - Filloux,A
AU  - Matthews,S
DO  - 10.1016/j.bbapap.2016.07.010
EP  - 1505
PY  - 2016///
SN  - 0005-2795
SP  - 1500
TI  - Crystal structure of the CupB6 adhesive tip from the chaperone-usher family of pili from Pseudomonas aeruginosa
T2  - Biochimica et Biophysica Acta - Protein Structure
UR  - http://dx.doi.org/10.1016/j.bbapap.2016.07.010
UR  - http://hdl.handle.net/10044/1/38543
VL  - 1864
ER  -
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