Article
Kelly A. Mercier and John R. Cort contributed equally to this work.
Received: 12 June 2008; Revised: 3 December 2008; Accepted: 8 December 2008
10.1002/pro.62 About DOI
Structure and function of Pseudomonas aeruginosa protein PA1324 (21-170) |
| Kelly A. Mercier 1 a, John R. Cort 2 *, Michael A. Kennedy 3, Erin E. Lockert 2, Shuisong Ni 3, Matthew D. Shortridge 1, Robert Powers 1 * |
| 1Department of Chemistry, University of Nebraska-Lincoln, Lincoln, Nebraska 68588 2Pacific Northwest National Laboratory, Biological Sciences Division, Northeast Structural Genomics Consortium and Washington State University Tri Cities, Richland, Washington 99354 3Department of Chemistry and Biochemistry and Northeast Structural Genomics Consortium, Miami University, Oxford, Ohio 45056 |
| email: John R. Cort (john.cort@pnl.gov) Robert Powers (rpowers3@unl.edu) |
*Correspondence to John R. Cort, Pacific Northwest National Laboratory, PO Box 999, MSIN: K8-98, Richland, WA 99354
*Correspondence to Robert Powers, Department of Chemistry, 722 Hamilton Hall, University of Nebraska-Lincoln, Lincoln, NE 68588
aCurrent address: Laboratory of Structural Biology, National Institute of Environmental Health Sciences, 111 T. W. Alexander Drive, Durham, NC 27713
Kelly A. Mercier and John R. Cort contributed equally to this work.Funded by:
Protein Structure Initiative of the National Institutes of Health; Grant Number: U54 GM074958 Nebraska Tobacco Settlement Biomedical Research Development Funds, Nebraska EPSCoR, and an Eloise Gerry Fellowship from Sigma Delta Epsilon NIH; Grant Number: RR015468-01
| Keywords |
| Pseudomonas aeruginosa PA1324 NMR functional genomics NMR high-throughput screens protein-ligand binding protein-ligand co-structures structural biology structural genomics chemical proteomics protein structure initiative hypothetical proteins FAST-NMR Northeast Structural Genomics Consortium |
| 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. |
Received: 12 June 2008; Revised: 3 December 2008; Accepted: 8 December 2008
| Digital Object Identifier (DOI) |
10.1002/pro.62 About DOI
