7XP1

Crystal structure of PmiR from Pseudomonas aeruginosa

Summary for 7XP1

• Entry DOI: 10.2210/pdb7xp1/pdb
• Descriptor: Probable transcriptional regulator, ZINC ION, ALPHA-METHYLISOCITRIC ACID, ... (6 entities in total)
• Functional Keywords: pmir, 2-methylcitrate cycle, bacterial virulence, signaling protein
• Biological source: Pseudomonas aeruginosa PAO1
• Total number of polymer chains: 1
• Total formula weight: 25679.25

Authors

Zhang, Y.X.,Liang, H.H.,Gan, J.H. (deposition date: 2022-05-02, release date: 2023-04-12, Last modification date: 2023-11-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)