Structural highlights
Function
Q9HWU7_PSEAE
Publication Abstract from PubMed
Pseudomonas aeruginosa is a Gram-negative opportunistic bacterial pathogen that can cause chronic infection of the lungs of cystic fibrosis patients. Chaperone-usher systems in P. aeruginosa are known to translocate and assemble adhesive pili on the bacterial surface and contribute to biofilm formation within the host. Here, we report the crystal structure of the tip adhesion subunit CupB6 from the cupB1-6 gene cluster. The tip domain is connected to the pilus via the N-terminal donor strand from the main pilus subunit CupB1. Although the CupB6 adhesion domain bears structural features similar to other CU adhesins it displays an unusual polyproline helix adjacent to a prominent surface pocket, which are likely the site for receptor recognition.
Crystal structure of the CupB6 adhesive tip from the chaperone-usher family of pili from Pseudomonas aeruginosa.,Rasheed M, Garnett J, Perez-Dorado I, Muhl D, Filloux A, Matthews S Biochim Biophys Acta. 2016 Nov;1864(11):1500-5. doi:, 10.1016/j.bbapap.2016.07.010. Epub 2016 Jul 29. PMID:27481165[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rasheed M, Garnett J, Perez-Dorado I, Muhl D, Filloux A, Matthews S. Crystal structure of the CupB6 adhesive tip from the chaperone-usher family of pili from Pseudomonas aeruginosa. Biochim Biophys Acta. 2016 Nov;1864(11):1500-5. doi:, 10.1016/j.bbapap.2016.07.010. Epub 2016 Jul 29. PMID:27481165 doi:http://dx.doi.org/10.1016/j.bbapap.2016.07.010