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7CSY

Pseudomonas aeruginosa antitoxin HigA with higBA promoter

Summary for 7CSY
Entry DOI10.2210/pdb7csy/pdb
DescriptorHTH cro/C1-type domain-containing protein, DNA (28-MER), DNA (29-MER), ... (5 entities in total)
Functional Keywordsdimer, antitoxin-dna complex, antitoxin/dna
Biological sourcePseudomonas aeruginosa PAO1
More
Total number of polymer chains6
Total formula weight62856.68
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 citationSong, 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: 33346387
DOI: 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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数据于2024-11-06公开中

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