7CSY
Pseudomonas aeruginosa antitoxin HigA with higBA promoter
Summary for 7CSY
Entry DOI | 10.2210/pdb7csy/pdb |
Descriptor | HTH cro/C1-type domain-containing protein, DNA (28-MER), DNA (29-MER), ... (5 entities in total) |
Functional Keywords | dimer, antitoxin-dna complex, antitoxin/dna |
Biological source | Pseudomonas aeruginosa PAO1 More |
Total number of polymer chains | 6 |
Total formula weight | 62856.68 |
Authors | Song, Y.J.,Luo, G.H.,Bao, R. (deposition date: 2020-08-17, release date: 2021-01-13, Last modification date: 2024-05-29) |
Primary citation | Song, Y.,Luo, G.,Zhu, Y.,Li, T.,Li, C.,He, L.,Zhao, N.,Zhao, C.,Yang, J.,Huang, Q.,Mu, X.,Tang, X.,Kang, M.,Wu, S.,He, Y.,Bao, R. Pseudomonas aeruginosa antitoxin HigA functions as a diverse regulatory factor by recognizing specific pseudopalindromic DNA motifs. Environ.Microbiol., 23:1541-1558, 2021 Cited by PubMed Abstract: Type II toxin-antitoxin (TA) systems modulate many essential cellular processes in prokaryotic organisms. Recent studies indicate certain type II antitoxins also transcriptionally regulate other genes, besides neutralizing toxin activity. Herein, we investigated the diverse transcriptional repression properties of type II TA antitoxin PaHigA from Pseudomonas aeruginosa. Biochemical and functional analyses showed that PaHigA recognized variable pseudopalindromic DNA sequences and repressed expression of multiple genes. Furthermore, we presented high resolution structures of apo-PaHigA, PaHigA-P and PaHigA-P complex, describing how the rearrangements of the HTH domain accounted for the different DNA-binding patterns among HigA homologues. Moreover, we demonstrated that the N-terminal loop motion of PaHigA was associated with its apo and DNA-bound states, reflecting a switch mechanism regulating HigA antitoxin function. Collectively, this work extends our understanding of how the PaHigB/HigA system regulates multiple metabolic pathways to balance the growth and stress response in P. aeruginosa and could guide further development of anti-TA oriented strategies for pathogen treatment. PubMed: 33346387DOI: 10.1111/1462-2920.15365 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.29 Å) |
Structure validation
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