Structural basis for Mep2 ammonium transceptor activation by phosphorylation

Mep2 proteins are tightly regulated fungal ammonium transporters. Here, the authors report the crystal structures of closed states of Mep2 proteins and propose a model for their regulation by comparing them with the open ammonium transporters of bacteria.

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Autores principales:	Bert van den Berg, Anupama Chembath, Damien Jefferies, Arnaud Basle, Syma Khalid, Julian C. Rutherford
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/38be9cd246c54d59853331b888ec31e0
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spelling	oai:doaj.org-article:38be9cd246c54d59853331b888ec31e02021-12-02T15:35:41ZStructural basis for Mep2 ammonium transceptor activation by phosphorylation10.1038/ncomms113372041-1723https://doaj.org/article/38be9cd246c54d59853331b888ec31e02016-04-01T00:00:00Zhttps://doi.org/10.1038/ncomms11337https://doaj.org/toc/2041-1723Mep2 proteins are tightly regulated fungal ammonium transporters. Here, the authors report the crystal structures of closed states of Mep2 proteins and propose a model for their regulation by comparing them with the open ammonium transporters of bacteria.Bert van den BergAnupama ChembathDamien JefferiesArnaud BasleSyma KhalidJulian C. RutherfordNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Bert van den Berg Anupama Chembath Damien Jefferies Arnaud Basle Syma Khalid Julian C. Rutherford Structural basis for Mep2 ammonium transceptor activation by phosphorylation
description	Mep2 proteins are tightly regulated fungal ammonium transporters. Here, the authors report the crystal structures of closed states of Mep2 proteins and propose a model for their regulation by comparing them with the open ammonium transporters of bacteria.
format	article
author	Bert van den Berg Anupama Chembath Damien Jefferies Arnaud Basle Syma Khalid Julian C. Rutherford
author_facet	Bert van den Berg Anupama Chembath Damien Jefferies Arnaud Basle Syma Khalid Julian C. Rutherford
author_sort	Bert van den Berg
title	Structural basis for Mep2 ammonium transceptor activation by phosphorylation
title_short	Structural basis for Mep2 ammonium transceptor activation by phosphorylation
title_full	Structural basis for Mep2 ammonium transceptor activation by phosphorylation
title_fullStr	Structural basis for Mep2 ammonium transceptor activation by phosphorylation
title_full_unstemmed	Structural basis for Mep2 ammonium transceptor activation by phosphorylation
title_sort	structural basis for mep2 ammonium transceptor activation by phosphorylation
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/38be9cd246c54d59853331b888ec31e0
work_keys_str_mv	AT bertvandenberg structuralbasisformep2ammoniumtransceptoractivationbyphosphorylation AT anupamachembath structuralbasisformep2ammoniumtransceptoractivationbyphosphorylation AT damienjefferies structuralbasisformep2ammoniumtransceptoractivationbyphosphorylation AT arnaudbasle structuralbasisformep2ammoniumtransceptoractivationbyphosphorylation AT symakhalid structuralbasisformep2ammoniumtransceptoractivationbyphosphorylation AT juliancrutherford structuralbasisformep2ammoniumtransceptoractivationbyphosphorylation
_version_	1718386466125512704

Structural basis for Mep2 ammonium transceptor activation by phosphorylation

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