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-Structure paper
タイトル | Structure and function of an Arabidopsis thaliana sulfate transporter. |
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ジャーナル・号・ページ | Nat Commun, Vol. 12, Issue 1, Page 4455, Year 2021 |
掲載日 | 2021年7月22日 |
著者 | Lie Wang / Kehan Chen / Ming Zhou / |
PubMed 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. |
リンク | Nat Commun / PubMed:34294705 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.75 Å |
構造データ | EMDB-23351, PDB-7lhv: |
化合物 | ChemComp-S1P: ChemComp-SO4: ChemComp-LBN: ChemComp-HOH: |
由来 |
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キーワード | TRANSPORT PROTEIN / Sulfate transport / SLC26 / MEMBRANE PROTEIN |