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Crystal structure of the CupB6 adhesive tip from the chaperone-usher family of pili from Pseudomonas aeruginosa

DOI: 10.1016/j.bbapap.2016.07.010 DOI Help

Authors: Masooma Rasheed (Department of Life Sciences, Imperial College London) , James Garnett (Queen Mary University of London) , Inmaculada Pérez-Dorado (Department of Life Sciences, Imperial College London) , Daniela Muhl (Department of Life Sciences, Imperial College London) , Alain Filloux (Department of Life Sciences, Imperial College London) , Steve Matthews (Imperial College London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Biochimica Et Biophysica Acta (bba) - Proteins And Proteomics , VOL 1864 , PAGES 1500 - 1505

State: Published (Approved)
Published: November 2016
Diamond Proposal Number(s): 12579

Open Access Open Access

Abstract: 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.

Diamond Keywords: Bacteria

Subject Areas: Biology and Bio-materials, Medicine

Instruments: I02-Macromolecular Crystallography

Added On: 14/09/2016 10:33


Discipline Tags:

Pathogens Infectious Diseases Health & Wellbeing Structural biology Drug Discovery Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)