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6SLN

Structure of the RagAB peptide transporter

Summary for 6SLN
Entry DOI10.2210/pdb6sln/pdb
Related6SLI 6SLJ
DescriptorRagA protein, Lipoprotein RagB, GLN-THR-ALA-GLY-ALA-ASN-SER-GLN-ARG-GLY-SER-ALA-GLY, ... (8 entities in total)
Functional Keywordsouter membrane protein, bacteroidetes, tonb dependent transporter, membrane protein
Biological sourcePorphyromonas gingivalis (strain ATCC BAA-308 / W83)
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Total number of polymer chains6
Total formula weight338225.05
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 citationMadej, 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: 32393857
DOI: 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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数据于2024-10-30公开中

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