6SLJ
Structure of the RagAB peptide transporter
6SLJ の概要
| エントリーDOI | 10.2210/pdb6slj/pdb |
| 関連するPDBエントリー | 6SLI |
| 分子名称 | RagA protein, Lipoprotein RagB, ALA-SER-THR-THR-GLY-ALA-ASN-SER-GLN-ARG-GLY-SER-GLY, ... (8 entities in total) |
| 機能のキーワード | outer membrane protein, bacteroidetes, tonb dependent transporter, membrane protein |
| 由来する生物種 | Porphyromonas gingivalis (strain ATCC BAA-308 / W83) 詳細 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 338205.99 |
| 構造登録者 | |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.04 Å) |
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