+検索条件
-Structure paper
| タイトル | Structural snapshots of Pseudomonas aeruginosa LptBFG and LptBFGC reveal insights into lipopolysaccharide recognition and transport. |
|---|---|
| ジャーナル・号・ページ | Nat Commun, Vol. 16, Issue 1, Page 11384, Year 2025 |
| 掲載日 | 2025年12月17日 |
著者 | Francesco 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 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:41407669 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 3.26 - 3.61 Å |
| 構造データ | EMDB-47084, PDB-9doh: EMDB-47085, PDB-9dok: EMDB-47086, PDB-9doo: EMDB-47088, PDB-9doq: EMDB-47089, PDB-9dor: |
| 化合物 | ![]() ChemComp-3PE: |
| 由来 |
|
キーワード | LIPID TRANSPORT / LPS transporter |
ムービー
コントローラー
構造ビューア
万見文献について



著者

リンク











キーワード