7XA9
Structure of Arabidopsis thaliana CLCa
Summary for 7XA9
| Entry DOI | 10.2210/pdb7xa9/pdb |
| EMDB information | 33088 |
| Descriptor | Chloride channel protein CLC-a, NITRATE ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | nitrate, antiporter, transport protein, membrane protein |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 2 |
| Total formula weight | 177788.64 |
| Authors | Ji, S.,Jin, H.,Kaiming, Z.,Mingxing, W.,Shanshan, L.,Long, C. (deposition date: 2022-03-17, release date: 2023-03-22, Last modification date: 2025-06-18) |
| Primary citation | He, J.,Wang, M.,Li, S.,Chen, L.,Zhang, K.,She, J. Cryo-EM structure of the plant nitrate transporter AtCLCa reveals characteristics of the anion-binding site and the ATP-binding pocket. J.Biol.Chem., 299:102833-102833, 2023 Cited by PubMed Abstract: 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. PubMed: 36581207DOI: 10.1016/j.jbc.2022.102833 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.84 Å) |
Structure validation
Download full validation report
