6d9z

Publication Abstract from PubMed

Sulfur, most abundantly found in the environment as sulfate (SO4(2-)), 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 SO4(2-) at the molecular level is limited. CysZ has been described as a SO4(2-) permease, but its sequence family is without known structural precedent. Based on crystallographic structure information, SO4(2-) binding and flux experiments, we provide insight into the molecular mechanism of CysZ-mediated translocation of SO4(2-) 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.

Structure-based analysis of CysZ-mediated cellular uptake of sulfate.,Assur Sanghai Z, Liu Q, Clarke OB, Belcher-Dufrisne M, Wiriyasermkul P, Giese MH, 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 Elife. 2018 May 24;7. pii: 27829. doi: 10.7554/eLife.27829. PMID:29792261^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.