1XPN
NMR structure of P. aeruginosa protein PA1324: Northeast Structural Genomics Consortium target PaP1
Summary for 1XPN
Entry DOI | 10.2210/pdb1xpn/pdb |
NMR Information | BMRB: 6343 |
Descriptor | hypothetical protein PA1324 (1 entity in total) |
Functional Keywords | b-barrel, structural genomics, northeast structural genomics consortium, nesg, protein structure initiative, psi, unknown function |
Biological source | Pseudomonas aeruginosa |
Total number of polymer chains | 1 |
Total formula weight | 18403.20 |
Authors | Cort, J.R.,Ni, S.,Lockert, E.E.,Montelione, G.T.,Kennedy, M.A.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2004-10-08, release date: 2004-11-23, Last modification date: 2024-03-06) |
Primary citation | Mercier, K.A.,Cort, J.R.,Kennedy, M.A.,Lockert, E.E.,Ni, S.,Shortridge, M.D.,Powers, R. Structure and function of Pseudomonas aeruginosa protein PA1324 (21-170). Protein Sci., 18:606-618, 2009 Cited by PubMed 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. PubMed: 19241370DOI: 10.1002/pro.62 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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