Structural basis for functional interactions in dimers of SLC26 transporters

Yung-Ning Chang; Eva A. Jaumann; Katrin Reichel; Julia Hartmann; Dominik Oliver; Gerhard Hummer; Benesh Joseph; Eric R. Geertsma

doi:10.1038/s41467-019-10001-w

Nature Communications (May 2019)

Structural basis for functional interactions in dimers of SLC26 transporters

Yung-Ning Chang,
Eva A. Jaumann,
Katrin Reichel,
Julia Hartmann,
Dominik Oliver,
Gerhard Hummer,
Benesh Joseph,
Eric R. Geertsma

Affiliations

Yung-Ning Chang: Institute of Biochemistry, Biocenter, Goethe University Frankfurt
Eva A. Jaumann: Institute of Physical and Theoretical Chemistry, Goethe University Frankfurt
Katrin Reichel: Department of Theoretical Biophysics, Max Planck Institute of Biophysics
Julia Hartmann: Department of Neurophysiology, Institute of Physiology and Pathophysiology, Philipps University
Dominik Oliver: Department of Neurophysiology, Institute of Physiology and Pathophysiology, Philipps University
Gerhard Hummer: Department of Theoretical Biophysics, Max Planck Institute of Biophysics
Benesh Joseph: Institute of Physical and Theoretical Chemistry, Goethe University Frankfurt
Eric R. Geertsma: Institute of Biochemistry, Biocenter, Goethe University Frankfurt

DOI: https://doi.org/10.1038/s41467-019-10001-w
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 10

Abstract

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The SLC26 family of transporters maintains anion equilibria in all kingdoms of life. Here, the authors resolve the structure of an SLC26 dimer embedded in a lipid membrane and characterize it by PELDOR/DEER distance measurements, biochemical studies with MD simulations and spin-label ensemble refinement.

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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