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5K21

Pyocyanin demethylase

Summary for 5K21
Entry DOI10.2210/pdb5k21/pdb
DescriptorPyocyanin demethylase, phenazin-1-ol, CALCIUM ION, ... (4 entities in total)
Functional Keywordsdemethylase phenazine, oxidoreductase
Biological sourceMycobacterium fortuitum subsp. fortuitum DSM 46621 = ATCC 6841
Total number of polymer chains3
Total formula weight46377.79
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 citationCosta, 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: 27940577
DOI: 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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