9G58
Pseudomonas fluorescens periplasmic aspartic peptidase Pfl01_1762 (RloA)
Summary for 9G58
| Entry DOI | 10.2210/pdb9g58/pdb |
| Descriptor | Putative ATP-dependent zinc protease domain-containing protein (2 entities in total) |
| Functional Keywords | retropepsin-like, periplasm, bacteria, hydrolase |
| Biological source | Pseudomonas fluorescens Pf0-1 |
| Total number of polymer chains | 2 |
| Total formula weight | 34791.73 |
| Authors | Lormand, J.D.,Sondermann, H. (deposition date: 2024-07-16, release date: 2025-04-09, Last modification date: 2025-04-16) |
| Primary citation | Lormand, J.D.,Savelle, C.H.,Teschler, J.K.,Lopez, E.,Little, R.H.,Malone, J.,Yildiz, F.H.,Garcia-Garcia, M.J.,Sondermann, H. Secreted retropepsin-like enzymes are essential for stress tolerance and biofilm formation in Pseudomonas aeruginosa. Biorxiv, 2025 Cited by PubMed Abstract: Proteases regulate important biological functions. Here we present the structural and functional characterization of three previously uncharacterized aspartic proteases in . We show that these proteases have structural hallmarks of retropepsin peptidases and play redundant roles for cell survival under hypoosmotic stress conditions. Consequently, we named them retropepsin-like osmotic stress tolerance peptidases (Rlo). Our research shows that while Rlo proteases are homologous to RimB, an aspartic peptidase involved in rhizosphere colonization and plant infection, they contain N-terminal signal peptides and perform distinct biological functions. Mutants lacking all three secreted Rlo peptidases show defects in antibiotic resistance, biofilm formation, and cell morphology. These defects are rescued by mutations in the inactive transglutaminase transmembrane protein RloB and the cytoplasmic ATP-grasp protein RloC, two previously uncharacterized genes in the same operon as one of the Rlo proteases. These studies identify Rlo proteases and operon products as critical factors in clinically relevant processes, making them appealing targets for therapeutic strategies against infections. PubMed: 40166241DOI: 10.1101/2025.03.18.643919 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
Download full validation report
