Rab1-AMPylation by Legionella DrrA is allosterically activated by Rab1

The Legionella effector DrrA AMPylates the host protein Rab1 during infection, but the mechanism is still under debate. Here, the authors provide structural insights into the low-affinity DrrA:Rab1 interaction, showing that Rab1 allosterically activates DrrA through a non-conventional binding mechan...

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Autores principales:	Jiqing Du, Marie-Kristin von Wrisberg, Burak Gulen, Matthias Stahl, Christian Pett, Christian Hedberg, Kathrin Lang, Sabine Schneider, Aymelt Itzen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/db46eaf2179e4b49abbf39b105a93816
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spelling	oai:doaj.org-article:db46eaf2179e4b49abbf39b105a938162021-12-02T11:50:29ZRab1-AMPylation by Legionella DrrA is allosterically activated by Rab110.1038/s41467-020-20702-22041-1723https://doaj.org/article/db46eaf2179e4b49abbf39b105a938162021-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20702-2https://doaj.org/toc/2041-1723The Legionella effector DrrA AMPylates the host protein Rab1 during infection, but the mechanism is still under debate. Here, the authors provide structural insights into the low-affinity DrrA:Rab1 interaction, showing that Rab1 allosterically activates DrrA through a non-conventional binding mechanism.Jiqing DuMarie-Kristin von WrisbergBurak GulenMatthias StahlChristian PettChristian HedbergKathrin LangSabine SchneiderAymelt ItzenNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Jiqing Du Marie-Kristin von Wrisberg Burak Gulen Matthias Stahl Christian Pett Christian Hedberg Kathrin Lang Sabine Schneider Aymelt Itzen Rab1-AMPylation by Legionella DrrA is allosterically activated by Rab1
description	The Legionella effector DrrA AMPylates the host protein Rab1 during infection, but the mechanism is still under debate. Here, the authors provide structural insights into the low-affinity DrrA:Rab1 interaction, showing that Rab1 allosterically activates DrrA through a non-conventional binding mechanism.
format	article
author	Jiqing Du Marie-Kristin von Wrisberg Burak Gulen Matthias Stahl Christian Pett Christian Hedberg Kathrin Lang Sabine Schneider Aymelt Itzen
author_facet	Jiqing Du Marie-Kristin von Wrisberg Burak Gulen Matthias Stahl Christian Pett Christian Hedberg Kathrin Lang Sabine Schneider Aymelt Itzen
author_sort	Jiqing Du
title	Rab1-AMPylation by Legionella DrrA is allosterically activated by Rab1
title_short	Rab1-AMPylation by Legionella DrrA is allosterically activated by Rab1
title_full	Rab1-AMPylation by Legionella DrrA is allosterically activated by Rab1
title_fullStr	Rab1-AMPylation by Legionella DrrA is allosterically activated by Rab1
title_full_unstemmed	Rab1-AMPylation by Legionella DrrA is allosterically activated by Rab1
title_sort	rab1-ampylation by legionella drra is allosterically activated by rab1
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/db46eaf2179e4b49abbf39b105a93816
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Rab1-AMPylation by Legionella DrrA is allosterically activated by Rab1

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