7LHV

Structure of Arabidopsis thaliana sulfate transporter AtSULTR4;1

Summary for 7LHV

• Entry DOI: 10.2210/pdb7lhv/pdb
• EMDB information: 23351
• Descriptor: Sulfate transporter 4.1, chloroplastic, (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate, SULFATE ION, ... (5 entities in total)
• Functional Keywords: sulfate transport, slc26, membrane protein, transport protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Total number of polymer chains: 2
• Total formula weight: 153566.49

Authors

Wang, L.,Chen, K.,Zhou, M. (deposition date: 2021-01-26, release date: 2021-08-11, Last modification date: 2025-05-28)

Primary citation

Wang, L.,Chen, K.,Zhou, M.
Structure and function of an Arabidopsis thaliana sulfate transporter.
Nat Commun, 12:4455-4455, 2021

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 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.

PubMed: 34294705
DOI: 10.1038/s41467-021-24778-2

Experimental method

ELECTRON MICROSCOPY (2.75 Å)