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

Kelly A. Mercier, John R. Cort, Michael A. Kennedy, Erin E. Lockert, Ni Shuisong, Matthew D. Shortridge, Robert Powers

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)606-618
Number of pages13
JournalProtein Science
Issue number3
StatePublished - Mar 2009


  • Chemical proteomics
  • Functional genomics
  • Hypothetical proteins
  • NMR
  • NMR high-throughput screens
  • Northeast structural genomics consortium
  • Protein structure initiative
  • Protein-ligand binding
  • Protein-ligand co-structures
  • Pseudomonas aeruginosa PA1324
  • Structural biology
  • Structural genomics

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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