6SLN
Structure of the RagAB peptide transporter
Summary for 6SLN
Entry DOI | 10.2210/pdb6sln/pdb |
Related | 6SLI 6SLJ |
Descriptor | RagA protein, Lipoprotein RagB, GLN-THR-ALA-GLY-ALA-ASN-SER-GLN-ARG-GLY-SER-ALA-GLY, ... (8 entities in total) |
Functional Keywords | outer membrane protein, bacteroidetes, tonb dependent transporter, membrane protein |
Biological source | Porphyromonas gingivalis (strain ATCC BAA-308 / W83) More |
Total number of polymer chains | 6 |
Total formula weight | 338225.05 |
Authors | Madej, M.,Ranson, N.A.,White, J.B.R. (deposition date: 2019-08-20, release date: 2020-05-20, Last modification date: 2024-01-24) |
Primary citation | Madej, M.,White, J.B.R.,Nowakowska, Z.,Rawson, S.,Scavenius, C.,Enghild, J.J.,Bereta, G.P.,Pothula, K.,Kleinekathoefer, U.,Basle, A.,Ranson, N.A.,Potempa, J.,van den Berg, B. Structural and functional insights into oligopeptide acquisition by the RagAB transporter from Porphyromonas gingivalis. Nat Microbiol, 5:1016-1025, 2020 Cited by PubMed 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 RagAB 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. PubMed: 32393857DOI: 10.1038/s41564-020-0716-y PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.61 Å) |
Structure validation
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