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-Structure paper
Title | Structure and function of an Arabidopsis thaliana sulfate transporter. |
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Journal, issue, pages | Nat Commun, Vol. 12, Issue 1, Page 4455, Year 2021 |
Publish date | Jul 22, 2021 |
Authors | Lie Wang / Kehan Chen / Ming Zhou / |
PubMed Abstract | Plant sulfate transporters (SULTR) mediate absorption and distribution of sulfate (SO) and are essential for plant growth; however, our understanding of their structures and functions remains ...Plant sulfate transporters (SULTR) mediate absorption and distribution of sulfate (SO) 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 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 is coordinated by side-chain hydroxyls and backbone amides, and further stabilized electrostatically by the conserved Arg393 and two helix dipoles. Proton and SO are co-transported by AtSULTR4;1 and a proton gradient significantly enhances SO transport. Glu347, which is ~7 Å from the bound SO, 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 transport, suggesting a regulatory function of the STAS domain. |
External links | Nat Commun / PubMed:34294705 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.75 Å |
Structure data | EMDB-23351, PDB-7lhv: |
Chemicals | ChemComp-S1P: ChemComp-SO4: ChemComp-LBN: ChemComp-HOH: |
Source |
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Keywords | TRANSPORT PROTEIN / Sulfate transport / SLC26 / MEMBRANE PROTEIN |