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Crystal structure of Type IX secretion system PorE C-terminal domain from Porphyromonas gingivalis in complex with a peptidoglycan fragment

Porphyromonas gingivalis, the major human pathogen associated to periodontal diseases, utilizes the Bacteroidetes-specific type IX secretion system (T9SS) to export virulence factors. PorE is a periplasmic multi-domain lipoprotein associated to the outer membrane that was recently identified as esse...

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Main Authors: Nhung Thi Trang Trinh, Hieu Quang Tran, Quyen Van Dong, Christian Cambillau, Alain Roussel, Philippe Leone
Format: Bài trích
Language:eng
Published: Scientific Reports 2021
Subjects:
Bacterial pathogenesis
Bacterial secretion
X-ray crystallography
Online Access:https://www.nature.com/articles/s41598-020-64115-z
https://dlib.phenikaa-uni.edu.vn/handle/PNK/2817
https://doi.org/10.1038/s41598-020-64115-z
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spelling oai:localhost:PNK-28172022-08-17T05:54:48Z Crystal structure of Type IX secretion system PorE C-terminal domain from Porphyromonas gingivalis in complex with a peptidoglycan fragment Nhung Thi Trang Trinh Hieu Quang Tran Quyen Van Dong Christian Cambillau Alain Roussel Philippe Leone Bacterial pathogenesis Bacterial secretion X-ray crystallography Porphyromonas gingivalis, the major human pathogen associated to periodontal diseases, utilizes the Bacteroidetes-specific type IX secretion system (T9SS) to export virulence factors. PorE is a periplasmic multi-domain lipoprotein associated to the outer membrane that was recently identified as essential for T9SS function. Little is known on T9SS at the structural level, and in particular its interaction with peptidoglycan. This prompted us to carry out structural studies on PorE full length as well as on its four isolated domains. Here we report the crystal structure of the C-terminal OmpA_C-like putative peptidoglycan-binding domain at 1.55?� resolution. An electron density volume was identified in the protein cleft, making it possible to build a naturally-occurring peptidoglycan fragment. This result suggests that PorE interacts with peptidoglycan and that PorE could anchor T9SS to the cell wall. 2021-09-13T04:24:47Z 2021-09-13T04:24:47Z 2021 Bài trích https://www.nature.com/articles/s41598-020-64115-z https://dlib.phenikaa-uni.edu.vn/handle/PNK/2817 https://doi.org/10.1038/s41598-020-64115-z eng application/pdf Scientific Reports
institution Digital Phenikaa
collection Digital Phenikaa
language eng
topic Bacterial pathogenesis
Bacterial secretion
X-ray crystallography
spellingShingle Bacterial pathogenesis
Bacterial secretion
X-ray crystallography
Nhung Thi Trang Trinh
Hieu Quang Tran
Quyen Van Dong
Christian Cambillau
Alain Roussel
Philippe Leone
Crystal structure of Type IX secretion system PorE C-terminal domain from Porphyromonas gingivalis in complex with a peptidoglycan fragment
description Porphyromonas gingivalis, the major human pathogen associated to periodontal diseases, utilizes the Bacteroidetes-specific type IX secretion system (T9SS) to export virulence factors. PorE is a periplasmic multi-domain lipoprotein associated to the outer membrane that was recently identified as essential for T9SS function. Little is known on T9SS at the structural level, and in particular its interaction with peptidoglycan. This prompted us to carry out structural studies on PorE full length as well as on its four isolated domains. Here we report the crystal structure of the C-terminal OmpA_C-like putative peptidoglycan-binding domain at 1.55?� resolution. An electron density volume was identified in the protein cleft, making it possible to build a naturally-occurring peptidoglycan fragment. This result suggests that PorE interacts with peptidoglycan and that PorE could anchor T9SS to the cell wall.
format Bài trích
author Nhung Thi Trang Trinh
Hieu Quang Tran
Quyen Van Dong
Christian Cambillau
Alain Roussel
Philippe Leone
author_facet Nhung Thi Trang Trinh
Hieu Quang Tran
Quyen Van Dong
Christian Cambillau
Alain Roussel
Philippe Leone
author_sort Nhung Thi Trang Trinh
title Crystal structure of Type IX secretion system PorE C-terminal domain from Porphyromonas gingivalis in complex with a peptidoglycan fragment
title_short Crystal structure of Type IX secretion system PorE C-terminal domain from Porphyromonas gingivalis in complex with a peptidoglycan fragment
title_full Crystal structure of Type IX secretion system PorE C-terminal domain from Porphyromonas gingivalis in complex with a peptidoglycan fragment
title_fullStr Crystal structure of Type IX secretion system PorE C-terminal domain from Porphyromonas gingivalis in complex with a peptidoglycan fragment
title_full_unstemmed Crystal structure of Type IX secretion system PorE C-terminal domain from Porphyromonas gingivalis in complex with a peptidoglycan fragment
title_sort crystal structure of type ix secretion system pore c-terminal domain from porphyromonas gingivalis in complex with a peptidoglycan fragment
publisher Scientific Reports
publishDate 2021
url https://www.nature.com/articles/s41598-020-64115-z
https://dlib.phenikaa-uni.edu.vn/handle/PNK/2817
https://doi.org/10.1038/s41598-020-64115-z
_version_ 1751856263782727680
score 8.887836

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