8B0V

Crystal structure of C-terminal domain of Pseudomonas aeruginosa LexA G91D mutant

Summary for 8B0V

• Entry DOI: 10.2210/pdb8b0v/pdb
• Related: 7ZZM
• EMDB information: 15038
• Descriptor: LexA repressor, 1,2-ETHANEDIOL, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: transcriptional regulator, serine-lysine protease, transcription
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 2
• Total formula weight: 28354.84

Authors

Vascon, F.,De Felice, S.,Chinellato, M.,Maso, L.,Cendron, L. (deposition date: 2022-09-08, release date: 2024-03-27, 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

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

Experimental method

X-RAY DIFFRACTION (1.7 Å)