Structure and function of Pseudomonas aeruginosa protein PA1324 (21–170)

✍ Scribed by Kelly A. Mercier; John R. Cort; Michael A. Kennedy; Erin E. Lockert; Shuisong Ni; Matthew D. Shortridge; Robert Powers

• Book ID: 105356628
• Publisher: Cold Spring Harbor Laboratory Press
• Year: 2009
• Tongue: English
• Weight: 507 KB
• Volume: 18
• Category: Article
• ISSN: 0961-8368
• DOI: 10.1002/pro.62

✦ Synopsis

Abstract

Pseudomonas aeruginosa is the prototypical biofilm‐forming gram‐negative opportunistic human pathogen. P. aeruginosa is causatively associated with nosocomial infections and with cystic fibrosis. Antibiotic resistance in some strains adds to the inherent difficulties that result from biofilm formation when treating P. aeruginosa infections. Transcriptional profiling studies suggest widespread changes in the proteome during quorum sensing and biofilm development. Many of the proteins found to be upregulated during these processes are poorly characterized from a functional standpoint. Here, we report the solution NMR structure of PA1324, a protein of unknown function identified in these studies, and provide a putative biological functional assignment based on the observed prealbumin‐like fold and FAST‐NMR ligand screening studies. PA1324 is postulated to be involved in the binding and transport of sugars or polysaccharides associated with the peptidoglycan matrix during biofilm formation.