National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)
DK122784
米国
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)
HL086392
米国
引用
ジャーナル: Nat Commun / 年: 2021 タイトル: Structure and function of an Arabidopsis thaliana sulfate transporter. 著者: Lie Wang / Kehan Chen / Ming Zhou / 要旨: 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.
履歴
登録
2021年1月26日
登録サイト: RCSB / 処理サイト: RCSB
改定 1.0
2021年8月11日
Provider: repository / タイプ: Initial release
改定 1.1
2024年5月29日
Group: Data collection / カテゴリ: chem_comp_atom / chem_comp_bond