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8S70

Cryo-EM structure of Pseudomonas aeruginosa recombinase A (RecA) in complex with ssDNA 72mer and ATPgS

Summary for 8S70
Entry DOI10.2210/pdb8s70/pdb
EMDB information19761
DescriptorProtein RecA, DNA, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordsrecombinase, co-protease activator, dna binding protein
Biological sourcePseudomonas aeruginosa
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Total number of polymer chains2
Total formula weight36781.43
Authors
De Felice, S.,Vascon, F.,Huber, S.T.,Grinzato, A.,Jakobi, A.J.,Cendron, L. (deposition date: 2024-02-28, release date: 2025-01-15, Last modification date: 2025-03-12)
Primary citationVascon, F.,De Felice, S.,Gasparotto, M.,Huber, S.T.,Catalano, C.,Chinellato, M.,Mezzetti, R.,Grinzato, A.,Filippini, F.,Maso, L.,Jakobi, A.J.,Cendron, L.
Snapshots of Pseudomonas aeruginosa SOS response reveal structural requisites for LexA autoproteolysis.
Iscience, 28:111726-111726, 2025
Cited by
PubMed Abstract: Antimicrobial resistance poses a severe threat to human health and stands out among the pathogens responsible for this emergency. The SOS response to DNA damage is crucial in bacterial evolution, influencing resistance development and adaptability in challenging environments, especially under antibiotic exposure. Recombinase A (RecA) and the transcriptional repressor LexA are the key players that orchestrate this process, determining either the silencing or the active transcription of the genes under their control. By integrating state-of-the-art structural approaches with binding and functional assays, we elucidated the molecular events activating the SOS response in , focusing on the RecA-LexA interaction. Our findings identify the conserved determinants and strength of the interactions that allow RecA to trigger LexA autocleavage and inactivation. These results provide the groundwork for designing novel antimicrobial strategies and exploring the potential translation of -derived approaches, to address the implications of infections.
PubMed: 39898034
DOI: 10.1016/j.isci.2024.111726
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.2 Å)
Structure validation

237735

数据于2025-06-18公开中

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