Structural basis for arginine glycosylation of host substrates by bacterial effector proteins

The type III secretion system effectors NleB and SseK are glycosyltransferases (GT) that specifically glycosylate arginine residues. Here the authors provide insights into their mechanism by combining X-ray crystallography, NMR, enzyme kinetics measurements, molecular dynamics simulations and in viv...

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Autores principales:	Jun Bae Park, Young Hun Kim, Youngki Yoo, Juyeon Kim, Sung-Hoon Jun, Jin Won Cho, Samir El Qaidi, Samuel Walpole, Serena Monaco, Ana A. García-García, Miaomiao Wu, Michael P. Hays, Ramon Hurtado-Guerrero, Jesus Angulo, Philip R. Hardwidge, Jeon-Soo Shin, Hyun-Soo Cho
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/49a452b7d1ba4b249efc0b07a970adb6
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spelling	oai:doaj.org-article:49a452b7d1ba4b249efc0b07a970adb62021-12-02T17:31:30ZStructural basis for arginine glycosylation of host substrates by bacterial effector proteins10.1038/s41467-018-06680-62041-1723https://doaj.org/article/49a452b7d1ba4b249efc0b07a970adb62018-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-06680-6https://doaj.org/toc/2041-1723The type III secretion system effectors NleB and SseK are glycosyltransferases (GT) that specifically glycosylate arginine residues. Here the authors provide insights into their mechanism by combining X-ray crystallography, NMR, enzyme kinetics measurements, molecular dynamics simulations and in vivo experiments and show that SseK/NleB enzymes are retaining GTs.Jun Bae ParkYoung Hun KimYoungki YooJuyeon KimSung-Hoon JunJin Won ChoSamir El QaidiSamuel WalpoleSerena MonacoAna A. García-GarcíaMiaomiao WuMichael P. HaysRamon Hurtado-GuerreroJesus AnguloPhilip R. HardwidgeJeon-Soo ShinHyun-Soo ChoNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-15 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Jun Bae Park Young Hun Kim Youngki Yoo Juyeon Kim Sung-Hoon Jun Jin Won Cho Samir El Qaidi Samuel Walpole Serena Monaco Ana A. García-García Miaomiao Wu Michael P. Hays Ramon Hurtado-Guerrero Jesus Angulo Philip R. Hardwidge Jeon-Soo Shin Hyun-Soo Cho Structural basis for arginine glycosylation of host substrates by bacterial effector proteins
description	The type III secretion system effectors NleB and SseK are glycosyltransferases (GT) that specifically glycosylate arginine residues. Here the authors provide insights into their mechanism by combining X-ray crystallography, NMR, enzyme kinetics measurements, molecular dynamics simulations and in vivo experiments and show that SseK/NleB enzymes are retaining GTs.
format	article
author	Jun Bae Park Young Hun Kim Youngki Yoo Juyeon Kim Sung-Hoon Jun Jin Won Cho Samir El Qaidi Samuel Walpole Serena Monaco Ana A. García-García Miaomiao Wu Michael P. Hays Ramon Hurtado-Guerrero Jesus Angulo Philip R. Hardwidge Jeon-Soo Shin Hyun-Soo Cho
author_facet	Jun Bae Park Young Hun Kim Youngki Yoo Juyeon Kim Sung-Hoon Jun Jin Won Cho Samir El Qaidi Samuel Walpole Serena Monaco Ana A. García-García Miaomiao Wu Michael P. Hays Ramon Hurtado-Guerrero Jesus Angulo Philip R. Hardwidge Jeon-Soo Shin Hyun-Soo Cho
author_sort	Jun Bae Park
title	Structural basis for arginine glycosylation of host substrates by bacterial effector proteins
title_short	Structural basis for arginine glycosylation of host substrates by bacterial effector proteins
title_full	Structural basis for arginine glycosylation of host substrates by bacterial effector proteins
title_fullStr	Structural basis for arginine glycosylation of host substrates by bacterial effector proteins
title_full_unstemmed	Structural basis for arginine glycosylation of host substrates by bacterial effector proteins
title_sort	structural basis for arginine glycosylation of host substrates by bacterial effector proteins
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/49a452b7d1ba4b249efc0b07a970adb6
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Structural basis for arginine glycosylation of host substrates by bacterial effector proteins

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