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

Assur Sanghai, Zahra, Liu, Qun, Clarke, Oliver B, Belcher-Dufrisne, Meagan, Wiriyasermkul, Pattama, Giese, M Hunter, Leal-Pinto, Edgar, Kloss, Brian, Tabuso, Shantelle, Love, James, Punta, Marco, Banerjee, Surajit, Rajashankar, Kanagalaghatta R, Rost, Burkhard, Logothetis, Diomedes, Quick, Matthias, Hendrickson, Wayne A, Mancia, Filippo·2018·eLife
DOI 10.7554/elife.27829PMC PMC5967866

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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.

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  • Such a dual topology architecture is exceedingly rare among membrane proteins, and has only been structurally confirmed for two other transporter classes.

    “Such an architecture is exceedingly rare among membrane proteins, and has only been structurally confirmed for two other transporter classes (71, 72).”

    From Membrane exporters of fluoride ion (2021) · cites this paper as [72]

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Metadata

Authors
Assur Sanghai, Z., Liu, Q., Clarke, O. B., Belcher-Dufrisne, M., Wiriyasermkul, P., Giese, M. H., Leal-Pinto, E., Kloss, B., Tabuso, S., Love, J., Punta, M., Banerjee, S., Rajashankar, K. R., Rost, B., Logothetis, D., Quick, M., Hendrickson, W. A., & Mancia, F.
Affiliations
  • Department of Physiology and Cellular Biophysics, Columbia University, New York, United States
  • Biology Department, Brookhaven National Laboratory, Upton, United States
  • Department of Biochemistry and Molecular Biophysics, Columbia University, New York, United States
  • Center for Molecular Recognition, Department of Psychiatry, Columbia University, New York, United States
  • Department of Physiology and Biophysics, Virginia Commonwealth University School of Medicine, Richmond, United States
  • New York Structural Biology Center, New York, United States
  • Centre for Evolution and Cancer, The Institute of Cancer Research, London, United Kingdom
  • Department of Chemistry and Chemical Biology, Cornell University, NE-CAT, Argonne, United States
  • Department of Informatics, Technical University of Munich, Munich, Germany
ORCID
Venue
eLife
Publisher
eLife Sciences Publications, Ltd
Published
2018-05-24
Volume
7
ISSN
2050-084X
DOI
10.7554/elife.27829
PMC
PMC5967866
Cited by
18
References
1
Language
en
Licence
Funders
  • National Institute of General Medical Sciences (R01 GM119396, R01 GM107462, U54 GM095315, P41 GM116799, R01 GM098617)
  • New York Consortium on Membrane Protein Structure (NYCOMPS; U54 GM095315)

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