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TitleCryo-EM structure of the plant nitrate transporter AtCLCa reveals characteristics of the anion-binding site and the ATP-binding pocket.
Journal, issue, pagesJ Biol Chem, Vol. 299, Issue 2, Page 102833, Year 2023
Publish dateDec 26, 2022
AuthorsJin He / Mingxing Wang / Shanshan Li / Long Chen / Kaiming Zhang / Ji She /
PubMed AbstractNitrate is one of the major nitrogen sources for most plants. Chloride channel (CLC) proteins mediate the transport and vacuole storage of nitrate in plants, but the structural basis of nitrate ...Nitrate is one of the major nitrogen sources for most plants. Chloride channel (CLC) proteins mediate the transport and vacuole storage of nitrate in plants, but the structural basis of nitrate transport by plant CLC proteins remains unknown. Here, we solved the cryo-EM structure of ATP-bound Arabidopsis thaliana CLCa (AtCLCa) at 2.8 Å resolution. Structural comparison between nitrate-selective AtCLCa and chloride-selective CLC-7 reveals key differences in the central anion-binding site. We observed that the central nitrate is shifted by ∼1.4 Å from chloride, which is likely caused by a weaker interaction between the anion and Pro160; the side chains of aromatic residues around the central binding site are rearranged to accommodate the larger nitrate. Additionally, we identified the ATP-binding pocket of AtCLCa to be located between the cytosolic cystathionine β-synthase domains and the N-terminus. The N-terminus may mediate the ATP inhibition of AtCLCa by interacting with both ATP and the pore-forming transmembrane helix. Together, our studies provide insights into the nitrate selectivity and ATP regulation of plant CLCs.
External linksJ Biol Chem / PubMed:36581207 / PubMed Central
MethodsEM (single particle)
Resolution2.84 Å
Structure data

33088

7xa9

EMDB-33088, PDB-7xa9:
Structure of Arabidopsis thaliana CLCa
Method: EM (single particle) / Resolution: 2.84 Å

Chemicals

ChemComp-NO3:
NITRATE ION / Nitrate

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-MG:
Unknown entry

Source
  • arabidopsis thaliana (thale cress)
KeywordsMEMBRANE PROTEIN / nitrate / antiporter / transport protein

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