7VOJ
Al-bound structure of the AtALMT1 mutant M60A
Summary for 7VOJ
| Entry DOI | 10.2210/pdb7voj/pdb |
| EMDB information | 32050 |
| Descriptor | Aluminum-activated malate transporter 1, ACETIC ACID, ALUMINUM ION (3 entities in total) |
| Functional Keywords | almt1, aluminum resistance, malate transport, transport protein |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 2 |
| Total formula weight | 113841.27 |
| Authors | Wang, J. (deposition date: 2021-10-14, release date: 2021-12-01, Last modification date: 2024-06-19) |
| Primary citation | Wang, J.,Yu, X.,Ding, Z.J.,Zhang, X.,Luo, Y.,Xu, X.,Xie, Y.,Li, X.,Yuan, T.,Zheng, S.J.,Yang, W.,Guo, J. Structural basis of ALMT1-mediated aluminum resistance in Arabidopsis. Cell Res., 32:89-98, 2022 Cited by PubMed Abstract: The plant aluminum (Al)-activated malate transporter ALMT1 mediates the efflux of malate to chelate the Al in acidic soils and underlies the plant Al resistance. Here we present cryo-electron microscopy (cryo-EM) structures of Arabidopsis thaliana ALMT1 (AtALMT1) in the apo, malate-bound, and Al-bound states at neutral and/or acidic pH at up to 3.0 Å resolution. The AtALMT1 dimer assembles an anion channel and each subunit contains six transmembrane helices (TMs) and six cytosolic α-helices. Two pairs of Arg residues are located in the center of the channel pore and contribute to malate recognition. Al binds at the extracellular side of AtALMT1 and induces conformational changes of the TM1-2 loop and the TM5-6 loop, resulting in the opening of the extracellular gate. These structures, along with electrophysiological measurements, molecular dynamic simulations, and mutagenesis study in Arabidopsis, elucidate the structural basis for Al-activated malate transport by ALMT1. PubMed: 34799726DOI: 10.1038/s41422-021-00587-6 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
Download full validation report
