9EYD

Structural basis of specific lysine transport by Pseudomonas aeruginosa permease LysP

9EYD の概要

• エントリーDOI: 10.2210/pdb9eyd/pdb
• EMDBエントリー: 50053
• 分子名称: Lysine-specific permease, Nanobody CA5755, LYSINE (3 entities in total)
• 機能のキーワード: complex, membrane protein
• 由来する生物種: Pseudomonas aeruginosa PAO1; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66407.63

構造登録者

Nji, E.,Matsuoka, R. (登録日: 2024-04-09, 公開日: 2025-10-29, 最終更新日: 2025-12-17)

主引用文献

Bicer, D.,Matsuoka, R.,Moumbock, A.F.A.,Sukumar, P.,Suades, A.,Cheruvara, H.,Quigley, A.,Drew, D.,Pardon, E.,Steyaert, J.,Henderson, P.J.F.,Caffrey, M.,Griese, J.J.,Nji, E.
Structural basis of specific lysine transport by Pseudomonas aeruginosa permease LysP.
Nat Commun, 2025

PubMed Abstract: Under conditions of extreme acidity, the lysine-specific permease, LysP, not only mediates the import of L-lysine it also interacts with the transcriptional regulator, CadC, to activate expression of the cadAB operon. This operon encodes the lysine decarboxylase, CadA, which converts lysine to cadaverine while consuming a cytoplasmic proton, and the antiporter, CadB, which exports protonated cadaverine in exchange for extracellular lysine. Together, these processes contribute to cytoplasmic pH homeostasis and support bacterial acid resistance - a mechanism essential for the survival of pathogenic bacteria in acidic host environments. Here, we present the cryo-EM structure of LysP from Pseudomonas aeruginosa in an inward-occluded conformation (3.2-5.3 Å resolution), bound to L-lysine and a nanobody. L-Lysine is coordinated by hydrophobic contacts, cation-π interactions, and by hydrogen bonding mostly with polar uncharged residues. Reconstitution of LysP into proteoliposomes confirms specific L-lysine transport, which is competitively inhibited by L-4-thialysine. These findings provide a structural framework for understanding selective lysine recognition and inhibition, with implications for antibacterial drug design.

PubMed: 41345107
DOI: 10.1038/s41467-025-66618-7

実験手法

ELECTRON MICROSCOPY (3.68 Å)