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Open data
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Basic information
| Entry | Database: PDB / ID: 8y6j | ||||||
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| Title | The structure of Oryza sativa HKT1;1 | ||||||
Components | Cation transporter HKT1;1,Soluble cytochrome b562 | ||||||
Keywords | PLANT PROTEIN / dimer / transmembrane protein / sodium transporter / BRIL-fused | ||||||
| Function / homology | Function and homology informationsodium ion transmembrane transporter activity / monoatomic cation transmembrane transporter activity / sodium ion transmembrane transport / electron transport chain / periplasmic space / electron transfer activity / iron ion binding / heme binding / plasma membrane Similarity search - Function | ||||||
| Biological species | ![]() ![]() | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.46 Å | ||||||
Authors | Yang, G.H. / Gao, R. | ||||||
| Funding support | China, 1items
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Citation | Journal: J Integr Plant Biol / Year: 2024Title: Structural insights into the Oryza sativa cation transporters HKTs in salt tolerance. Authors: Ran Gao / Yutian Jia / Xia Xu / Peng Fu / Jiaqi Zhou / Guanghui Yang / ![]() 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 ...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. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8y6j.cif.gz | 179.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb8y6j.ent.gz | 138.4 KB | Display | PDB format |
| PDBx/mmJSON format | 8y6j.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8y6j_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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| Full document | 8y6j_full_validation.pdf.gz | 1.2 MB | Display | |
| Data in XML | 8y6j_validation.xml.gz | 33.2 KB | Display | |
| Data in CIF | 8y6j_validation.cif.gz | 47.6 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/y6/8y6j ftp://data.pdbj.org/pub/pdb/validation_reports/y6/8y6j | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 38988MC ![]() 8y6lC ![]() 8y6mC ![]() 8y6nC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 73833.484 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: HKT1;1, HKT4, Os04g0607500, LOC_Os04g51820, OSJNBa0060N03.3, cybC Production host: Homo sapiens (human) / References: UniProt: Q7XPF8, UniProt: P0ABE7Has protein modification | Y | |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Structure of OsHKT1;1 / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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| Source (natural) | Organism: ![]() |
| Source (recombinant) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 8 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: OTHER |
| Electron lens | Mode: DIFFRACTION / Nominal defocus max: 1800 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
| CTF correction | Type: NONE |
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| 3D reconstruction | Resolution: 3.46 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 292396 / Symmetry type: POINT |
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China, 1items
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Homo sapiens (human)
FIELD EMISSION GUN