Combining several structural biology methods, researchers at the Biozentrum, University of Basel, have revealed the structure of the BAM-darobactin complex at the molecular level. The study could have a significant impact on the search for new antibiotics to fight pathogens.
In a study published in Nature, scientists from the Biozentrum, University of Basel describe the mechanism of action of Darobactin, a molecule, which selectively kills Gram-negative pathogens and presents a very promising lead substance for the development of a new antibiotic.
They resolve how Darobactin interacts with the BAM membrane protein complex using a combination of cryo-electron microscopy, X-ray crystallography, native mass spectrometry, in vivo experiments and molecular dynamics simulations. The crystallographic data were collected at the X06Sa-PXI beamline at the Swiss Light Source.
Contact
Dr. Takashi Tomizaki
Swiss Light Source
Paul Scherrer Institute PSI
+41 56 310 5129
takashi.tomizaki@psi.ch
Media release
Publications
The antibiotic darobactin mimics a β-strand to inhibit outer membrane insertase
Hundeep Kaur, Roman P. Jakob, Jan K. Marzinek, Robert Green, Yu Imai,
Jani Reddy Bolla, Elia Agustoni, Carol V. Robinson, Peter J. Bond, Kim Lewis, Timm Maier and Sebastian Hiller
https://doi.org/10.1038/s41586-021-03455-w