8S70
Cryo-EM structure of Pseudomonas aeruginosa recombinase A (RecA) in complex with ssDNA 72mer and ATPgS
Summary for 8S70
Entry DOI | 10.2210/pdb8s70/pdb |
EMDB information | 19761 |
Descriptor | Protein RecA, DNA, MAGNESIUM ION, ... (4 entities in total) |
Functional Keywords | recombinase, co-protease activator, dna binding protein |
Biological source | Pseudomonas aeruginosa More |
Total number of polymer chains | 2 |
Total formula weight | 36781.43 |
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 citation | Vascon, 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: 39898034DOI: 10.1016/j.isci.2024.111726 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.2 Å) |
Structure validation
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