5K21
Pyocyanin demethylase
Summary for 5K21
| Entry DOI | 10.2210/pdb5k21/pdb |
| Descriptor | Pyocyanin demethylase, phenazin-1-ol, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | demethylase phenazine, oxidoreductase |
| Biological source | Mycobacterium fortuitum subsp. fortuitum DSM 46621 = ATCC 6841 |
| Total number of polymer chains | 3 |
| Total formula weight | 46377.79 |
| Authors | Costa, K.C.,Glasser, N.R.,Newman, D.K. (deposition date: 2016-05-18, release date: 2016-12-07, Last modification date: 2024-11-20) |
| Primary citation | Costa, K.C.,Glasser, N.R.,Conway, S.J.,Newman, D.K. Pyocyanin degradation by a tautomerizing demethylase inhibits Pseudomonas aeruginosa biofilms. Science, 355:170-173, 2017 Cited by PubMed Abstract: The opportunistic pathogen Pseudomonas aeruginosa produces colorful redox-active metabolites called phenazines, which underpin biofilm development, virulence, and clinical outcomes. Although phenazines exist in many forms, the best studied is pyocyanin. Here, we describe pyocyanin demethylase (PodA), a hitherto uncharacterized protein that oxidizes the pyocyanin methyl group to formaldehyde and reduces the pyrazine ring via an unusual tautomerizing demethylation reaction. Treatment with PodA disrupts P. aeruginosa biofilm formation similarly to DNase, suggesting interference with the pyocyanin-dependent release of extracellular DNA into the matrix. PodA-dependent pyocyanin demethylation also restricts established biofilm aggregate populations experiencing anoxic conditions. Together, these results show that modulating extracellular redox-active metabolites can influence the fitness of a biofilm-forming microorganism. PubMed: 27940577DOI: 10.1126/science.aag3180 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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