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Structural and functional insights into oligopeptide acquisition by the RagAB transporter from Porphyromonas gingivalis

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Structural and functional insights into oligopeptide acquisition by the RagAB transporter from Porphyromonas gingivalis. / Madej, Mariusz; White, Joshua B. R.; Nowakowska, Zuzanna; Rawson, Shaun; Scavenius, Carsten; Enghild, Jan J.; Bereta, Grzegorz P.; Pothula, Karunakar; Kleinekathoefer, Ulrich; Basle, Arnaud; Ranson, Neil A.; Potempa, Jan; van den Berg, Bert.

I: Nature Microbiology, Bind 5, Nr. 8, 08.2020, s. 1016-1025.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Madej, M, White, JBR, Nowakowska, Z, Rawson, S, Scavenius, C, Enghild, JJ, Bereta, GP, Pothula, K, Kleinekathoefer, U, Basle, A, Ranson, NA, Potempa, J & van den Berg, B 2020, 'Structural and functional insights into oligopeptide acquisition by the RagAB transporter from Porphyromonas gingivalis', Nature Microbiology, bind 5, nr. 8, s. 1016-1025. https://doi.org/10.1038/s41564-020-0716-y

APA

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. (2020). Structural and functional insights into oligopeptide acquisition by the RagAB transporter from Porphyromonas gingivalis. Nature Microbiology, 5(8), 1016-1025. https://doi.org/10.1038/s41564-020-0716-y

CBE

Madej M, White JBR, Nowakowska Z, Rawson S, Scavenius C, Enghild JJ, Bereta GP, Pothula K, Kleinekathoefer U, Basle A, Ranson NA, Potempa J, van den Berg B. 2020. Structural and functional insights into oligopeptide acquisition by the RagAB transporter from Porphyromonas gingivalis. Nature Microbiology. 5(8):1016-1025. https://doi.org/10.1038/s41564-020-0716-y

MLA

Vancouver

Author

Madej, Mariusz ; White, Joshua B. R. ; Nowakowska, Zuzanna ; Rawson, Shaun ; Scavenius, Carsten ; Enghild, Jan J. ; Bereta, Grzegorz P. ; Pothula, Karunakar ; Kleinekathoefer, Ulrich ; Basle, Arnaud ; Ranson, Neil A. ; Potempa, Jan ; van den Berg, Bert. / Structural and functional insights into oligopeptide acquisition by the RagAB transporter from Porphyromonas gingivalis. I: Nature Microbiology. 2020 ; Bind 5, Nr. 8. s. 1016-1025.

Bibtex

@article{aee0e253f6fc40debb8b213eec995369,
title = "Structural and functional insights into oligopeptide acquisition by the RagAB transporter from Porphyromonas gingivalis",
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 RagA(2)B(2) 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.Porphyromonas gingivalis, an oral anaerobe involved in the pathogenesis of periodontitis, relies on extracellular proteases to degrade proteins into peptides for growth, but how these peptides enter the cell is unknown. Here, the authors identify RagAB as the outer-membrane importer for these peptides and solve its structure, elucidating that it works via a 'pedal bin' mechanism of nutrient uptake.",
keywords = "MEMBRANE, PERIODONTITIS, DYNAMICS, PROTEIN, IMPLEMENTATION, RECOGNITION, VALIDATION, MODULATION, UPDATE, SYSTEM",
author = "Mariusz Madej and White, {Joshua B. R.} and Zuzanna Nowakowska and Shaun Rawson and Carsten Scavenius and Enghild, {Jan J.} and Bereta, {Grzegorz P.} and Karunakar Pothula and Ulrich Kleinekathoefer and Arnaud Basle and Ranson, {Neil A.} and Jan Potempa and {van den Berg}, Bert",
year = "2020",
month = aug,
doi = "10.1038/s41564-020-0716-y",
language = "English",
volume = "5",
pages = "1016--1025",
journal = "Nature Microbiology",
issn = "2058-5276",
publisher = "Nature Publishing Group",
number = "8",

}

RIS

TY - JOUR

T1 - Structural and functional insights into oligopeptide acquisition by the RagAB transporter from Porphyromonas gingivalis

AU - Madej, Mariusz

AU - White, Joshua B. R.

AU - Nowakowska, Zuzanna

AU - Rawson, Shaun

AU - Scavenius, Carsten

AU - Enghild, Jan J.

AU - Bereta, Grzegorz P.

AU - Pothula, Karunakar

AU - Kleinekathoefer, Ulrich

AU - Basle, Arnaud

AU - Ranson, Neil A.

AU - Potempa, Jan

AU - van den Berg, Bert

PY - 2020/8

Y1 - 2020/8

N2 - 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 RagA(2)B(2) 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.Porphyromonas gingivalis, an oral anaerobe involved in the pathogenesis of periodontitis, relies on extracellular proteases to degrade proteins into peptides for growth, but how these peptides enter the cell is unknown. Here, the authors identify RagAB as the outer-membrane importer for these peptides and solve its structure, elucidating that it works via a 'pedal bin' mechanism of nutrient uptake.

AB - 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 RagA(2)B(2) 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.Porphyromonas gingivalis, an oral anaerobe involved in the pathogenesis of periodontitis, relies on extracellular proteases to degrade proteins into peptides for growth, but how these peptides enter the cell is unknown. Here, the authors identify RagAB as the outer-membrane importer for these peptides and solve its structure, elucidating that it works via a 'pedal bin' mechanism of nutrient uptake.

KW - MEMBRANE

KW - PERIODONTITIS

KW - DYNAMICS

KW - PROTEIN

KW - IMPLEMENTATION

KW - RECOGNITION

KW - VALIDATION

KW - MODULATION

KW - UPDATE

KW - SYSTEM

U2 - 10.1038/s41564-020-0716-y

DO - 10.1038/s41564-020-0716-y

M3 - Journal article

C2 - 32393857

VL - 5

SP - 1016

EP - 1025

JO - Nature Microbiology

JF - Nature Microbiology

SN - 2058-5276

IS - 8

ER -