Haysom, S.F., Machin, J., Whitehouse, J.M. et al. (9 more authors) (2023) Innentitelbild: Darobactin B Stabilises a Lateral‐Closed Conformation of the BAM Complex in E. coli Cells (Angew. Chem. 34/2023). Wiley.
Abstract
The β-barrel assembly machine (BAM) is essential for folding outer membrane proteins (OMPs) into the outer membrane (OM) of Gram-negative bacteria. Structures of BAM have been solved using X-ray crystallography and cryoEM, but the conformation of BAM in the highly crowded native OM remained unsolved. Using EPR spectroscopy of BAM in intact E. coli cells, the structure of BAM in situ has now been revealed in the Research Article (e202218783) by Sheena E. Radford, Christos Pliotas et al., both alone and in the presence of the antibacterial, darobactin B. Image: Jeroen Claus (Phospho Biomedical Animation).
Metadata
Item Type: | Other |
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Authors/Creators: |
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Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 13 May 2025 13:20 |
Last Modified: | 13 May 2025 13:20 |
Published Version: | https://onlinelibrary.wiley.com/doi/10.1002/ange.2... |
Status: | Published |
Publisher: | Wiley |
Identification Number: | 10.1002/ange.202308371 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:226558 |