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Open data
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Basic information
Entry | Database: PDB / ID: 8y6m | ||||||
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Title | The structure of Oryza sativa HKT2;1 | ||||||
![]() | Cation transporter HKT2;1,Soluble cytochrome b562 | ||||||
![]() | PLANT PROTEIN / sodium/potassium sympoter / homodomer / transmembrane protein / BRIL-fused | ||||||
Function / homology | ![]() monoatomic cation transmembrane transporter activity / inorganic cation transmembrane transport / sodium ion transport / electron transport chain / potassium ion transport / 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: 2.91 Å | ||||||
![]() | Yang, G.H. / Gao, R. / Jia, Y.T. / Xu, X. / Fu, P. / Zhou, J.Q. | ||||||
Funding support | ![]()
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![]() | ![]() Title: 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. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 174.3 KB | Display | ![]() |
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PDB format | ![]() | 134.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 38991MC ![]() 8y6jC ![]() 8y6lC ![]() 8y6nC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Components
#1: Protein | Mass: 70030.367 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() Gene: HKT2;1, HKT1, OsI_023492, cybC Production host: ![]() ![]() References: UniProt: A2YGP9, UniProt: P0ABE7 Has 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 Oryza sativa HKT2;1 / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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Source (natural) | Organism: ![]() ![]() |
Source (recombinant) | Organism: ![]() |
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: ![]() |
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 (6k x 4k) |
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Processing
CTF correction | Type: NONE |
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3D reconstruction | Resolution: 2.91 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 192005 / Symmetry type: POINT |