Structure-based analysis of CysZ-mediated cellular uptake of sulfate

Author:

Assur Sanghai Zahra12,Liu Qun3,Clarke Oliver B2ORCID,Belcher-Dufrisne Meagan1,Wiriyasermkul Pattama4,Giese M Hunter12,Leal-Pinto Edgar56,Kloss Brian7,Tabuso Shantelle7,Love James7,Punta Marco8,Banerjee Surajit9,Rajashankar Kanagalaghatta R9,Rost Burkhard10,Logothetis Diomedes56,Quick Matthias411,Hendrickson Wayne A127,Mancia Filippo1ORCID

Affiliation:

1. Department of Physiology and Cellular Biophysics, Columbia University, New York, United States

2. Department of Biochemistry and Molecular Biophysics, Columbia University, New York, United States

3. Biology Department, Brookhaven National Laboratory, Upton, United States

4. Center for Molecular Recognition, Department of Psychiatry, Columbia University, New York, United States

5. Department of Physiology and Biophysics, Virginia Commonwealth University School of Medicine, Richmond, United States

6. Department of Pharmaceutical Sciences, School of Pharmacy, Bouvé College of Health Sciences, Northeastern University, Boston, United States

7. New York Structural Biology Center, New York, United States

8. Centre for Evolution and Cancer, The Institute of Cancer Research, London, United Kingdom

9. Department of Chemistry and Chemical Biology, Cornell University, NE-CAT, Argonne, United States

10. Department of Informatics, Technical University of Munich, Munich, Germany

11. Division of Molecular Therapeutics, New York State Psychiatric Institute, New York, United States

Abstract

Sulfur, most abundantly found in the environment as sulfate (SO42-), is an essential element in metabolites required by all living cells, including amino acids, co-factors and vitamins. However, current understanding of the cellular delivery of SO42- at the molecular level is limited. CysZ has been described as a SO42- permease, but its sequence family is without known structural precedent. Based on crystallographic structure information, SO42- binding and flux experiments, we provide insight into the molecular mechanism of CysZ-mediated translocation of SO42- across membranes. CysZ structures from three different bacterial species display a hitherto unknown fold and have subunits organized with inverted transmembrane topology. CysZ from Pseudomonas denitrificans assembles as a trimer of antiparallel dimers and the CysZ structures from two other species recapitulate dimers from this assembly. Mutational studies highlight the functional relevance of conserved CysZ residues.

Funder

National Institute of General Medical Sciences

New York Consortium on Membrane Protein Structure

Publisher

eLife Sciences Publications, Ltd

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,General Medicine,General Neuroscience

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