Anchoring the T6SS to the cell wall: Crystal structure of the peptidoglycan binding domain of the TagL accessory protein.

The type VI secretion system (T6SS) is a widespread mechanism of protein delivery into target cells, present in more than a quarter of all sequenced Gram-negative bacteria. The T6SS constitutes an important virulence factor, as it is responsible for targeting effectors in both prokaryotic and eukary...

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Autores principales:	Van Son Nguyen, Silvia Spinelli, Éric Cascales, Alain Roussel, Christian Cambillau, Philippe Leone
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/6644a051d5e3427090bdfde3ffd63472
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spelling	oai:doaj.org-article:6644a051d5e3427090bdfde3ffd634722021-12-02T20:15:38ZAnchoring the T6SS to the cell wall: Crystal structure of the peptidoglycan binding domain of the TagL accessory protein.1932-620310.1371/journal.pone.0254232https://doaj.org/article/6644a051d5e3427090bdfde3ffd634722021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0254232https://doaj.org/toc/1932-6203The type VI secretion system (T6SS) is a widespread mechanism of protein delivery into target cells, present in more than a quarter of all sequenced Gram-negative bacteria. The T6SS constitutes an important virulence factor, as it is responsible for targeting effectors in both prokaryotic and eukaryotic cells. The T6SS comprises a tail structure tethered to the cell envelope via a trans-envelope complex. In most T6SS, the membrane complex is anchored to the cell wall by the TagL accessory protein. In this study, we report the first crystal structure of a peptidoglycan-binding domain of TagL. The fold is conserved with members of the OmpA/Pal/MotB family, and more importantly, the peptidoglycan binding site is conserved. This structure further exemplifies how proteins involved in anchoring to the cell wall for different cellular functions rely on an interaction network with peptidoglycan strictly conserved.Van Son NguyenSilvia SpinelliÉric CascalesAlain RousselChristian CambillauPhilippe LeonePublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 7, p e0254232 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Van Son Nguyen Silvia Spinelli Éric Cascales Alain Roussel Christian Cambillau Philippe Leone Anchoring the T6SS to the cell wall: Crystal structure of the peptidoglycan binding domain of the TagL accessory protein.
description	The type VI secretion system (T6SS) is a widespread mechanism of protein delivery into target cells, present in more than a quarter of all sequenced Gram-negative bacteria. The T6SS constitutes an important virulence factor, as it is responsible for targeting effectors in both prokaryotic and eukaryotic cells. The T6SS comprises a tail structure tethered to the cell envelope via a trans-envelope complex. In most T6SS, the membrane complex is anchored to the cell wall by the TagL accessory protein. In this study, we report the first crystal structure of a peptidoglycan-binding domain of TagL. The fold is conserved with members of the OmpA/Pal/MotB family, and more importantly, the peptidoglycan binding site is conserved. This structure further exemplifies how proteins involved in anchoring to the cell wall for different cellular functions rely on an interaction network with peptidoglycan strictly conserved.
format	article
author	Van Son Nguyen Silvia Spinelli Éric Cascales Alain Roussel Christian Cambillau Philippe Leone
author_facet	Van Son Nguyen Silvia Spinelli Éric Cascales Alain Roussel Christian Cambillau Philippe Leone
author_sort	Van Son Nguyen
title	Anchoring the T6SS to the cell wall: Crystal structure of the peptidoglycan binding domain of the TagL accessory protein.
title_short	Anchoring the T6SS to the cell wall: Crystal structure of the peptidoglycan binding domain of the TagL accessory protein.
title_full	Anchoring the T6SS to the cell wall: Crystal structure of the peptidoglycan binding domain of the TagL accessory protein.
title_fullStr	Anchoring the T6SS to the cell wall: Crystal structure of the peptidoglycan binding domain of the TagL accessory protein.
title_full_unstemmed	Anchoring the T6SS to the cell wall: Crystal structure of the peptidoglycan binding domain of the TagL accessory protein.
title_sort	anchoring the t6ss to the cell wall: crystal structure of the peptidoglycan binding domain of the tagl accessory protein.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/6644a051d5e3427090bdfde3ffd63472
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Anchoring the T6SS to the cell wall: Crystal structure of the peptidoglycan binding domain of the TagL accessory protein.

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