Structural basis for Mep2 ammonium transceptor activation by phosphorylation

Bert van den Berg; Anupama Chembath; Damien Jefferies; Arnaud Basle; Syma Khalid; Julian C. Rutherford

doi:10.1038/ncomms11337

Nature Communications (Apr 2016)

Structural basis for Mep2 ammonium transceptor activation by phosphorylation

Bert van den Berg,
Anupama Chembath,
Damien Jefferies,
Arnaud Basle,
Syma Khalid,
Julian C. Rutherford

Affiliations

Bert van den Berg: Institute for Cell and Molecular Biosciences, The Medical School, Newcastle University
Anupama Chembath: Institute for Cell and Molecular Biosciences, The Medical School, Newcastle University
Damien Jefferies: School of Chemistry, University of Southampton
Arnaud Basle: Institute for Cell and Molecular Biosciences, The Medical School, Newcastle University
Syma Khalid: School of Chemistry, University of Southampton
Julian C. Rutherford: Institute for Cell and Molecular Biosciences, The Medical School, Newcastle University

DOI: https://doi.org/10.1038/ncomms11337
Journal volume & issue: Vol. 7, no. 1
pp. 1 – 11

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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