Madej, M, White, JBR, Nowakowska, Z et al. (10 more authors) (2020) Structural and functional insights into oligopeptide acquisition by the RagAB transporter from Porphyromonas gingivalis. Nature Microbiology, 5 (8). pp. 1016-1025. ISSN 2058-5276
Abstract
Porphyromonas gingivalis, an asaccharolytic member of the Bacteroidetes, is a keystone pathogen in human periodontitis that may also contribute to the development of other chronic inflammatory diseases. P. gingivalis utilizes protease-generated peptides derived from extracellular proteins for growth, but how these peptides enter the cell is not clear. Here, we identify RagAB as the outer-membrane importer for these peptides. X-ray crystal structures show that the transporter forms a dimeric RagA2B2 complex, with the RagB substrate-binding surface-anchored lipoprotein forming a closed lid on the RagA TonB-dependent transporter. Cryo-electron microscopy structures reveal the opening of the RagB lid and thus provide direct evidence for a ‘pedal bin’ mechanism of nutrient uptake. Together with mutagenesis, peptide-binding studies and RagAB peptidomics, our work identifies RagAB as a dynamic, selective outer-membrane oligopeptide-acquisition machine that is essential for the efficient utilization of proteinaceous nutrients by P. gingivalis.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © The Author(s), under exclusive licence to Springer Nature Limited 2020. This is an author produced version of an article published in Nature Microbiology. Uploaded in accordance with the publisher's self-archiving policy. |
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) > Cryo EM, Image Processing (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 11 Jun 2020 11:16 |
Last Modified: | 17 Nov 2020 18:13 |
Status: | Published |
Publisher: | Nature Research |
Identification Number: | 10.1038/s41564-020-0716-y |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:161770 |