The Pseudomonas aeruginosa substrate-binding protein Ttg2D functions as a general glycerophospholipid transporter across the periplasm
Yero et al. elucidate the function of Ttg2D, a Pseudomonas aeruginosa periplasmic protein, in maintaining phospholipid asymmetry between the outer and inner membrane. Gram negative bacteria have inner and outer membranes that differ in phospholipd composition. Using X-ray crystallography and mass sp...
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| Autores principales: | , , , , , , , , |
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| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
Nature Portfolio
2021
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/50977891a64d4ef6a08754ef5a6e7656 |
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| Sumario: | Yero et al. elucidate the function of Ttg2D, a Pseudomonas aeruginosa periplasmic protein, in maintaining phospholipid asymmetry between the outer and inner membrane. Gram negative bacteria have inner and outer membranes that differ in phospholipd composition. Using X-ray crystallography and mass spectrometry, the authors show that Ttg2D can carry two diacyl glycerophospholipids or a cardiolipin. The authors also identify a role for Ttg2D in resistance against antibiotics that use a lipid-mediated pathway into the cell. |
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