8Y6J
The structure of Oryza sativa HKT1;1
Summary for 8Y6J
| Entry DOI | 10.2210/pdb8y6j/pdb |
| EMDB information | 38988 |
| Descriptor | Cation transporter HKT1;1,Soluble cytochrome b562 (1 entity in total) |
| Functional Keywords | dimer, transmembrane protein, sodium transporter, bril-fused, plant protein |
| Biological source | Oryza sativa (Asian cultivated rice) More |
| Total number of polymer chains | 2 |
| Total formula weight | 147666.97 |
| Authors | |
| Primary citation | Gao, R.,Jia, Y.,Xu, X.,Fu, P.,Zhou, J.,Yang, G. Structural insights into the Oryza sativa cation transporters HKTs in salt tolerance. J Integr Plant Biol, 66:700-708, 2024 Cited by PubMed Abstract: The high-affinity potassium transporters (HKTs), selectively permeable to either Na alone or Na/K, play pivotal roles in maintaining plant Na/K homeostasis. Although their involvement in salt tolerance is widely reported, the molecular underpinnings of Oryza sativa HKTs remain elusive. In this study, we elucidate the structures of OsHKT1;1 and OsHKT2;1, representing two distinct classes of rice HKTs. The dimeric assembled OsHKTs can be structurally divided into four domains. At the dimer interface, a half-helix or a loop in the third domain is coordinated by the C-terminal region of the opposite subunit. Additionally, we present the structures of OsHKT1;5 salt-tolerant and salt-sensitive variants, a key quantitative trait locus associated with salt tolerance. The salt-tolerant variant of OsHKT1;5 exhibits enhanced Na transport capability and displays a more flexible conformation. These findings shed light on the molecular basis of rice HKTs and provide insights into their role in salt tolerance. PubMed: 38409933DOI: 10.1111/jipb.13632 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.46 Å) |
Structure validation
Download full validation report
