7XP1

Crystal structure of PmiR from Pseudomonas aeruginosa

7XP1 の概要

• エントリーDOI: 10.2210/pdb7xp1/pdb
• 分子名称: Probable transcriptional regulator, ZINC ION, ALPHA-METHYLISOCITRIC ACID, ... (6 entities in total)
• 機能のキーワード: pmir, 2-methylcitrate cycle, bacterial virulence, signaling protein
• 由来する生物種: Pseudomonas aeruginosa PAO1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25679.25

構造登録者

Zhang, Y.X.,Liang, H.H.,Gan, J.H. (登録日: 2022-05-02, 公開日: 2023-04-12, 最終更新日: 2023-11-29)

主引用文献

Cui, G.,Zhang, Y.,Xu, X.,Liu, Y.,Li, Z.,Wu, M.,Liu, J.,Gan, J.,Liang, H.
PmiR senses 2-methylisocitrate levels to regulate bacterial virulence in Pseudomonas aeruginosa.
Sci Adv, 8:eadd4220-eadd4220, 2022

PubMed Abstract: To adapt to changes in environmental cues, produces an array of virulence factors to survive the host immune responses during infection. Metabolic products contribute to bacterial virulence; however, only a limited number of these signaling receptors have been explored in detail for their ability to modulate virulence in bacteria. Here, we characterize the metabolic pathway of 2-methylcitrate cycle in and unveil that PmiR served as a receptor of 2-methylisocitrate (MIC) to govern bacterial virulence. Crystallographic studies and structural-guided mutagenesis uncovered several residues crucial for PmiR's allosteric activation by MIC. We also demonstrated that PmiR directly repressed the quorum-sensing system and subsequently inhibited pyocyanin production. Moreover, mutation of reduces bacterial survival in a mouse model of acute pneumonia infection. Collectively, this study identified PmiR as an important metabolic sensor for regulating expression of bacterial virulence genes to adapt to the harsh environments.

PubMed: 36475801
DOI: 10.1126/sciadv.add4220

実験手法

X-RAY DIFFRACTION (2.5 Å)