Year: 2021
Type: article
Abstract: Plant sulfate transporters (SULTR) mediate absorption and distribution of sulfate (SO 4 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 SO 4 2− at an overall resolution of 2.8 Å. AtSULTR4;1 forms a homodimer and has a structural fold typical of the SLC26 family of anion transporters. The bound SO 4 2− is coordinated by side-chain hydroxyls and backbone amides, and further stabilized electrostatically by the conserved Arg393 and two helix dipoles. Proton and SO 4 2− are co-transported by AtSULTR4;1 and a proton gradient significantly enhances SO 4 2− transport. Glu347, which is ~7 Å from the bound SO 4 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 SO 4 2− transport, suggesting a regulatory function of the STAS domain.
Source: Nature Communications
Authors: Lie Wang, Kehan Chen, Ming Zhou
Institution: Baylor College of Medicine
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $5,560
Awards: Structure and mechanism of mammalian stearoyl-CoA desaturases, Structural mechanism of K channel modulation by cellular redox state, G1820728362, G2647627320, Recruitment of Rising Stars, G356983052, G4075444098, G4391804966, G5049941135, Structure and Function of a Phosphorylation Coupled Saccharide Transporter, G9000153152, G9000269686
OpenAlex ID: W3183366938