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Open data
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Basic information
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Title | Oryza sativa HKT1;5 salt sensitive variant | |||||||||
![]() | open with UCSF-Chimera | |||||||||
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![]() | dimer / transmembrane protein / sodium transporter / BRIL-fused / MEMBRANE PROTEIN | |||||||||
Function / homology | ![]() regulation of sodium 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 | single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||
![]() | Yang GH / Gao R | |||||||||
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
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 59.5 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 13.8 KB 13.8 KB | Display Display | ![]() |
Images | ![]() | 38.8 KB | ||
Filedesc metadata | ![]() | 5.5 KB | ||
Others | ![]() ![]() | 59.3 MB 59.3 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8y6lMC ![]() 8y6jC ![]() 8y6mC ![]() 8y6nC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | open with UCSF-Chimera | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.04 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: open with UCSF-Chimera
File | emd_38990_half_map_1.map | ||||||||||||
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Annotation | open with UCSF-Chimera | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: open with UCSF-Chimera
File | emd_38990_half_map_2.map | ||||||||||||
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Annotation | open with UCSF-Chimera | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Structure of OsHKT1;5 salt sensitive variant
Entire | Name: Structure of OsHKT1;5 salt sensitive variant |
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Components |
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-Supramolecule #1: Structure of OsHKT1;5 salt sensitive variant
Supramolecule | Name: Structure of OsHKT1;5 salt sensitive variant / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Cation transporter HKT1;5,Soluble cytochrome b562
Macromolecule | Name: Cation transporter HKT1;5,Soluble cytochrome b562 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 70.901805 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MDYKDDDDKA SDEVDAGTMS SLDATTPRYD EFKRIYHLFL FHAHPFWLQL LYFLFISLLG FLMLKALPMK TSMVPRPMDL DLIFTSVSA TTVSSMVAVE MESFSNSQLL LITLLMLLGG EVFTSILGLY FTNAKYSSKM IARRQLADLE DNWETLNDNL K VIEKADNA ...String: MDYKDDDDKA SDEVDAGTMS SLDATTPRYD EFKRIYHLFL FHAHPFWLQL LYFLFISLLG FLMLKALPMK TSMVPRPMDL DLIFTSVSA TTVSSMVAVE MESFSNSQLL LITLLMLLGG EVFTSILGLY FTNAKYSSKM IARRQLADLE DNWETLNDNL K VIEKADNA AQVKDALTKM RAAALDAQKA TPPKLEDKSP DSPEMKDFRH GFDILVGQID DALKLANEGK VKEAQAAAEQ LK TTRNAYI QKYLERARST LSSASKTTTT RLLMFVVMGY HAVVHVAGYT AIVVYLSAVG GAGAVVAGKG ISAHTFAIFT VVS TFANCG FVPTNEGMVS FRSFPGLLLL VMPHVLLGNT LFPVFLRLAI AALERVTGWP ELGELLIRRR RGGGEGYHHL LPSS RTRFL ALTVAVLVVA QLALFCAMEW GSDGLRGLTA GQKLVGALFM AVNSRHSGEM VLDLSTVSSA VVVLYVVMMY LPPYT TFVP VQDKHQQTGA QSGQEGSSSS SIWQKLLMSP LSCLAIFIVV ICITERRQIA DDPINYSVLN IVVEVISAYG NVGFST GYS CARQVRPDGS CRDLWVGFSG KWSKQGKLTL MAVMFYGRLK KFSLHGGQAW KIEGSAWSHP QFEKGGGSGG GSGGSAW SH PQFEK UniProtKB: Cation transporter HKT1;5, Soluble cytochrome b562, Cation transporter HKT1;5 |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: OTHER / Imaging mode: DIFFRACTION / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.2 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 117768 |
Initial angle assignment | Type: ANGULAR RECONSTITUTION |
Final angle assignment | Type: ANGULAR RECONSTITUTION |