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Lookup NU author(s): Dr Augustinas SilaleORCiD, Dr Yiling Zhu, Dr Satya Bhamidimarri, Dr Arnaud Basle
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© 2023, The Author(s). The outer membrane (OM) in diderm, or Gram-negative, bacteria must be tethered to peptidoglycan for mechanical stability and to maintain cell morphology. Most diderm phyla from the Terrabacteria group have recently been shown to lack well-characterised OM attachment systems, but instead have OmpM, which could represent an ancestral tethering system in bacteria. Here, we have determined the structure of the most abundant OmpM protein from Veillonella parvula (diderm Firmicutes) by single particle cryogenic electron microscopy. We also characterised the channel properties of the transmembrane β-barrel of OmpM and investigated the structure and PG-binding properties of its periplasmic stalk region. Our results show that OM tethering and nutrient acquisition are genetically linked in V. parvula, and probably other diderm Terrabacteria. This dual function of OmpM may have played a role in the loss of the OM in ancestral bacteria and the emergence of monoderm bacterial lineages.
Author(s): Silale A, Zhu Y, Witwinowski J, Smith RE, Newman KE, Bhamidimarri SP, Basle A, Khalid S, Beloin C, Gribaldo S, van den Berg B
Publication type: Article
Publication status: Published
Journal: Nature Communications
Year: 2023
Volume: 14
Online publication date: 06/11/2023
Acceptance date: 16/10/2023
Date deposited: 20/11/2023
ISSN (electronic): 2041-1723
Publisher: Springer Nature
URL: https://doi.org/10.1038/s41467-023-42601-y
DOI: 10.1038/s41467-023-42601-y
Data Access Statement: Electron microscopy maps have been deposited in the Electron Microscopy Data Bank with the accession codes EMD-16328 (VpOmpM1 from E. coli in C1), EMD-16333 (VpOmpM1 from E. coli in C3) and EMD-16332 (VpOmpM1 from V. parvula in C1). Atomic coordinates have been deposited in the Protein Data Bank under accession codes 8BYM (VpOmpM1 from E. coli in C1), 8BYT (VpOmpM1 from E. coli in C3), 8BYS (VpOmpM1 from V. parvula in C1), and 8BZ2 (VpOmpM1 stalk crystal structure). The following atomic coordinates used for comparison purposes were downloaded from the Protein Data Bank: 3PYW, 6CWH, 3POQ, 5F7L, 2OMF, 2ZFG, 8AGD. Trajectories and run input files for the Molecular Dynamics simulations are available on Zenodo (https://doi.org/10.5281/zenodo.8239075). Source data for electrophysiology, liposome swelling assays, and HOLE and MD analyses are available. Other data presented in this paper, constructs and strains are available on reasonable request. Source data are provided with this paper.
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