Journal
STRUCTURE
Volume 18, Issue 2, Pages 265-273Publisher
CELL PRESS
DOI: 10.1016/j.str.2009.11.015
Keywords
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Funding
- Canadian Institutes of Health [AI-19146]
- National Institute of Allergy and Infectious Disease
- Cystic Fibrosis (CF) Foundation
- Veterans Administrations Medical Research Funds
- Canada Research Chair
- CIHR New Investigator award
- Natural Sciences and Engineering Research Council
- Canadian CIF Foundation
- Ontario Graduate Scholarship Program
- Ontario Student Opportunities Trust Fund
- Hospital for Sick Children Foundation
- US Department of Energy
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The opportunistic pathogen Pseudomonas aeruginosa causes chronic biofilm infections in cystic fibrosis patients. During colonization of the lung, A aeruginosa converts to a mucoid phenotype characterized by overproduction of the exopolysaccharide alginate. Here we show that AlgK, a protein essential for production of high molecular weight alginate, is an outer membrane lipoprotein that contributes to the correct localization of the porin AlgE. Our 2.5 angstrom structure shows AlgK is composed of 9.5 tetratricopeptide-like repeats, and three putative sites of protein-protein interaction have been identified. Bioinformatics analysis suggests that BcsA, PgaA, and PelB, involved in the production and export of cellulose, poly-beta-1,6-N-Acetyl-D-glucosamine, and Pel exopolysaccharide, respectively, share the same topology as AlgK/E. Together, our data suggest that AlgK plays a role in the assembly of the alginate biosynthetic complex and represents the periplasmic component of a new type of outer membrane secretin that differs from canonical bacterial capsular polysaccharide secretion systems.
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