8ARV
Structure of the EAL domain of BifA from Pseudomonas aeruginosa
Summary for 8ARV
Entry DOI | 10.2210/pdb8arv/pdb |
Descriptor | Bifunctional diguanylate cyclase/phosphodiesterase, MAGNESIUM ION (3 entities in total) |
Functional Keywords | eal domain, pde, phosphodiesterase, bifa, pseudomonas aeruginosa, c-di-gmp, hydrolase |
Biological source | Pseudomonas aeruginosa PAO1 |
Total number of polymer chains | 2 |
Total formula weight | 62323.17 |
Authors | Dias Teixeira, R.,Jenal, U.,Hiller, S. (deposition date: 2022-08-17, release date: 2023-04-12, Last modification date: 2024-05-01) |
Primary citation | Manner, C.,Dias Teixeira, R.,Saha, D.,Kaczmarczyk, A.,Zemp, R.,Wyss, F.,Jaeger, T.,Laventie, B.J.,Boyer, S.,Malone, J.G.,Qvortrup, K.,Andersen, J.B.,Givskov, M.,Tolker-Nielsen, T.,Hiller, S.,Drescher, K.,Jenal, U. A genetic switch controls Pseudomonas aeruginosa surface colonization. Nat Microbiol, 8:1520-1533, 2023 Cited by PubMed Abstract: Efficient colonization of mucosal surfaces is essential for opportunistic pathogens like Pseudomonas aeruginosa, but how bacteria collectively and individually adapt to optimize adherence, virulence and dispersal is largely unclear. Here we identified a stochastic genetic switch, hecR-hecE, which is expressed bimodally and generates functionally distinct bacterial subpopulations to balance P. aeruginosa growth and dispersal on surfaces. HecE inhibits the phosphodiesterase BifA and stimulates the diguanylate cyclase WspR to increase c-di-GMP second messenger levels and promote surface colonization in a subpopulation of cells; low-level HecE-expressing cells disperse. The fraction of HecE cells is tuned by different stress factors and determines the balance between biofilm formation and long-range cell dispersal of surface-grown communities. We also demonstrate that the HecE pathway represents a druggable target to effectively counter P. aeruginosa surface colonization. Exposing such binary states opens up new ways to control mucosal infections by a major human pathogen. PubMed: 37291227DOI: 10.1038/s41564-023-01403-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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