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Publication Abstract from PubMed

Plant sulfate transporters (SULTR) mediate absorption and distribution of sulfate (SO4(2-)) and are essential for plant growth; however, our understanding of their structures and functions remains inadequate. Here we present the structure of a SULTR from Arabidopsis thaliana, AtSULTR4;1, in complex with SO4(2-) at an overall resolution of 2.8 A. AtSULTR4;1 forms a homodimer and has a structural fold typical of the SLC26 family of anion transporters. The bound SO4(2-) is coordinated by side-chain hydroxyls and backbone amides, and further stabilized electrostatically by the conserved Arg393 and two helix dipoles. Proton and SO4(2-) are co-transported by AtSULTR4;1 and a proton gradient significantly enhances SO4(2-) transport. Glu347, which is ~7 A from the bound SO4(2-), is required for H(+)-driven transport. The cytosolic STAS domain interacts with transmembrane domains, and deletion of the STAS domain or mutations to the interface compromises dimer formation and reduces SO4(2-) transport, suggesting a regulatory function of the STAS domain.

Structure and function of an Arabidopsis thaliana sulfate transporter.,Wang L, Chen K, Zhou M Nat Commun. 2021 Jul 22;12(1):4455. doi: 10.1038/s41467-021-24778-2. PMID:34294705^[1]

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