6SML

Structure of the RagAB peptide importer in the 'open-open' state

6SML の概要

• エントリーDOI: 10.2210/pdb6sml/pdb
• 関連するPDBエントリー: 6SLI 6SLJ 6SLN 6SM3
• EMDBエントリー: 10241 10243
• 分子名称: Lipoprotein RagB, RagA protein, GLY-THR-GLY-GLY-SER-THR-GLY-THR-THR-SER-ALA-GLY, ... (5 entities in total)
• 機能のキーワード: beta-barrel, omp, tonb-dependent, transporter, membrane protein
• 由来する生物種: Porphyromonas gingivalis W83; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 158456.33

構造登録者

White, J.B.R.,Ranson, N.A.,van den Berg, B. (登録日: 2019-08-22, 公開日: 2020-05-20, 最終更新日: 2025-10-01)

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

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

実験手法

ELECTRON MICROSCOPY (3.4 Å)