The extracellular gate shapes the energy profile of an ABC exporter

ABC exporters hydrolyze ATP to pump substrates across membranes, but critical steps of the transport mechanism remain poorly understood. Here, the authors solve the crystal structure of outward-facing TM287/288 with the help of a state-specific sybody and gain insights into the role of the extracell...

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Autores principales:	Cedric A. J. Hutter, M. Hadi Timachi, Lea M. Hürlimann, Iwan Zimmermann, Pascal Egloff, Hendrik Göddeke, Svetlana Kucher, Saša Štefanić, Mikko Karttunen, Lars V. Schäfer, Enrica Bordignon, Markus A. Seeger
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/10e4f9ba103940ba80927107a3cf8a89
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spelling	oai:doaj.org-article:10e4f9ba103940ba80927107a3cf8a892021-12-02T14:39:35ZThe extracellular gate shapes the energy profile of an ABC exporter10.1038/s41467-019-09892-62041-1723https://doaj.org/article/10e4f9ba103940ba80927107a3cf8a892019-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-09892-6https://doaj.org/toc/2041-1723ABC exporters hydrolyze ATP to pump substrates across membranes, but critical steps of the transport mechanism remain poorly understood. Here, the authors solve the crystal structure of outward-facing TM287/288 with the help of a state-specific sybody and gain insights into the role of the extracellular gate.Cedric A. J. HutterM. Hadi TimachiLea M. HürlimannIwan ZimmermannPascal EgloffHendrik GöddekeSvetlana KucherSaša ŠtefanićMikko KarttunenLars V. SchäferEnrica BordignonMarkus A. SeegerNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Cedric A. J. Hutter M. Hadi Timachi Lea M. Hürlimann Iwan Zimmermann Pascal Egloff Hendrik Göddeke Svetlana Kucher Saša Štefanić Mikko Karttunen Lars V. Schäfer Enrica Bordignon Markus A. Seeger The extracellular gate shapes the energy profile of an ABC exporter
description	ABC exporters hydrolyze ATP to pump substrates across membranes, but critical steps of the transport mechanism remain poorly understood. Here, the authors solve the crystal structure of outward-facing TM287/288 with the help of a state-specific sybody and gain insights into the role of the extracellular gate.
format	article
author	Cedric A. J. Hutter M. Hadi Timachi Lea M. Hürlimann Iwan Zimmermann Pascal Egloff Hendrik Göddeke Svetlana Kucher Saša Štefanić Mikko Karttunen Lars V. Schäfer Enrica Bordignon Markus A. Seeger
author_facet	Cedric A. J. Hutter M. Hadi Timachi Lea M. Hürlimann Iwan Zimmermann Pascal Egloff Hendrik Göddeke Svetlana Kucher Saša Štefanić Mikko Karttunen Lars V. Schäfer Enrica Bordignon Markus A. Seeger
author_sort	Cedric A. J. Hutter
title	The extracellular gate shapes the energy profile of an ABC exporter
title_short	The extracellular gate shapes the energy profile of an ABC exporter
title_full	The extracellular gate shapes the energy profile of an ABC exporter
title_fullStr	The extracellular gate shapes the energy profile of an ABC exporter
title_full_unstemmed	The extracellular gate shapes the energy profile of an ABC exporter
title_sort	extracellular gate shapes the energy profile of an abc exporter
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/10e4f9ba103940ba80927107a3cf8a89
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The extracellular gate shapes the energy profile of an ABC exporter

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