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


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.

SUBMITTER: Assur Sanghai Z 

PROVIDER: S-EPMC5967866 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature

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Sulfur, most abundantly found in the environment as sulfate (SO<sub>4</sub><sup>2-</sup>), 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<sub>4</sub><sup>2-</sup> at the molecular level is limited. CysZ has been described as a SO<sub>4</sub><sup>2-</sup> permease, but its sequence family is without known structural precedent. Based on crystallographic structure info  ...[more]

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