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TitleStructural snapshots of Pseudomonas aeruginosa LptBFG and LptBFGC reveal insights into lipopolysaccharide recognition and transport.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 11384, Year 2025
Publish dateDec 17, 2025
AuthorsFrancesco Fiorentino / Matteo Cervoni / Yi Wang / Leonhard H Urner / Joshua B Sauer / Anh Tran / Robin A Corey / Dante Rotili / Antonello Mai / Phillip J Stansfeld / Francesco Imperi / Edward W Yu / Chih-Chia Su / Carol V Robinson / Jani R Bolla /
PubMed AbstractGram-negative bacteria are intrinsically resistant to many antibiotics because of densely packed lipopolysaccharides (LPS) in the outer leaflet of their outer membrane (OM), which acts as a highly ...Gram-negative bacteria are intrinsically resistant to many antibiotics because of densely packed lipopolysaccharides (LPS) in the outer leaflet of their outer membrane (OM), which acts as a highly effective barrier towards the spontaneous permeation of toxic molecules, including antibiotics. LPS are extracted from the inner membrane by the ABC transporter LptBFGC and translocated across the periplasm via a protein bridge to the OM. While structural studies have elucidated aspects of Lpt function in enterobacteria, little is known about how this system operates in divergent species such as Pseudomonas aeruginosa, a major human pathogen. Here, we report five cryo-electron microscopy structures of P. aeruginosa LptBFG and LptBFGC, revealing a rigid body movement in the periplasmic β-jellyroll domains necessary for LPS to shuttle through the periplasmic space. Notably, these structures exhibit a significantly smaller LPS binding cavity compared to previously determined models, suggesting the ligand-unbound states of the transporter. Mass spectrometry and molecular dynamics simulations indicate that the phosphate groups of LPS are the key determinants for binding and that the transporter can also accommodate cardiolipin. Together, these findings reveal previously unappreciated structural diversity in the Lpt system and provide mechanistic insight into how pathogenic Gram-negative bacteria tailor LPS recognition and transport. This understanding offers new avenues for the development of novel inhibitors targeting membrane biogenesis.
External linksNat Commun / PubMed:41407669 / PubMed Central
MethodsEM (single particle)
Resolution3.26 - 3.61 Å
Structure data

47084

9doh

EMDB-47084, PDB-9doh:
Cryo-EM structure of LptB2FG apo-1
Method: EM (single particle) / Resolution: 3.34 Å

47085

9dok

EMDB-47085, PDB-9dok:
Cryo-EM structure of LptB2FG apo-II
Method: EM (single particle) / Resolution: 3.26 Å

47086

9doo

EMDB-47086, PDB-9doo:
Cryo-EM structure of LptB2FG apo-III
Method: EM (single particle) / Resolution: 3.31 Å

47088

9doq

EMDB-47088, PDB-9doq:
Cryo-EM structure of LptB2FGC apo-I
Method: EM (single particle) / Resolution: 3.26 Å

47089

9dor

EMDB-47089, PDB-9dor:
Cryo-EM structure of LptB2FGC apo-II
Method: EM (single particle) / Resolution: 3.61 Å

Chemicals

ChemComp-3PE:
1,2-Distearoyl-sn-glycerophosphoethanolamine / phospholipid*YM

Source
  • pseudomonas aeruginosa (bacteria)
KeywordsLIPID TRANSPORT / LPS transporter

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