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Title | Structure-based analysis of CysZ-mediated cellular uptake of sulfate. |
Publication Type | Journal Article |
Year of Publication | 2018 |
Authors | Sanghai, ZAssur, Liu, Q, Clarke, OB, Belcher-Dufrisne, M, Wiriyasermkul, P, M Giese, H, Leal-Pinto, E, Kloss, B, Tabuso, S, Love, J, Punta, M, Banerjee, S, Rajashankar, KR, Rost, B, Logothetis, D, Quick, M, Hendrickson, WA, Mancia, F |
Journal | Elife |
Volume | 7 |
Date Published | 2018 May 24 |
ISSN | 2050-084X |
Abstract | Sulfur, most abundantly found in the environment as sulfate (SO), 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 SO at the molecular level is limited. CysZ has been described as a SO permease, but its sequence family is without known structural precedent. Based on crystallographic structure information, SO binding and flux experiments, we provide insight into the molecular mechanism of CysZ-mediated translocation of SO across membranes. CysZ structures from three different bacterial species display a hitherto unknown fold and have subunits organized with inverted transmembrane topology. CysZ from 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. |
DOI | 10.7554/eLife.27829 |
Alternate Journal | Elife |
PubMed ID | 29792261 |
PubMed Central ID | PMC5967866 |
Grant List | S10 RR029205 / RR / NCRR NIH HHS / United States P41 GM103403 / GM / NIGMS NIH HHS / United States P41 GM116799 / / National Institute of General Medical Sciences / R01 GM098617 / GM / NIGMS NIH HHS / United States R01 GM107462 / GM / NIGMS NIH HHS / United States R01 GM107462 / / National Institute of General Medical Sciences / P41 GM116799 / GM / NIGMS NIH HHS / United States U54 GM095315 / / National Institute of General Medical Sciences / R01 GM119396 / / National Institute of General Medical Sciences / U54 GM095315 / GM / NIGMS NIH HHS / United States R01 GM098617 / / National Institute of General Medical Sciences / R01 GM119396 / GM / NIGMS NIH HHS / United States NYCOMPS; U54 GM095315 / / New York Consortium on Membrane Protein Structure / |