9G59

Pseudomonas aeruginosa periplasmic aspartic peptidase PA0462 (RloA2)

9G59 の概要

• エントリーDOI: 10.2210/pdb9g59/pdb
• 分子名称: Putative ATP-dependent zinc protease domain-containing protein (2 entities in total)
• 機能のキーワード: retropepsin-like protease, periplasmic, bacteria, hydrolase
• 由来する生物種: Pseudomonas aeruginosa PAO1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34627.00

構造登録者

Lormand, J.D.,Sondermann, H. (登録日: 2024-07-16, 公開日: 2025-04-09, 最終更新日: 2025-04-16)

主引用文献

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

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: 40166241
DOI: 10.1101/2025.03.18.643919

実験手法

X-RAY DIFFRACTION (2.4 Å)