+Open data
-Basic information
Entry | Database: PDB / ID: 8w9v | ||||||
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Title | structure of TaHKT2;1 in KCl at 2.9 Angstroms resolution | ||||||
Components | HKT2 | ||||||
Keywords | TRANSPORT PROTEIN / HKT / ion selectivity / salt tolerance | ||||||
Function / homology | : / Cation transporter / Cation transport protein / metal ion transport / monoatomic cation transmembrane transporter activity / plasma membrane / : / Uncharacterized protein Function and homology information | ||||||
Biological species | Triticum aestivum (bread wheat) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.9 Å | ||||||
Authors | Wang, J. / Su, N. / Guo, J. | ||||||
Funding support | China, 1items
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Citation | Journal: Mol Plant / Year: 2024 Title: Structures and ion transport mechanisms of plant high-affinity potassium transporters. Authors: Jiangqin Wang / Yanping Luo / Fan Ye / Zhong Jie Ding / Shao Jian Zheng / Shuai Qiao / Yong Wang / Jiangtao Guo / Wei Yang / Nannan Su / Abstract: Plant high-affinity K transporters (HKTs) mediate Na and K uptake, maintain Na/K homeostasis, and therefore play crucial roles in plant salt tolerance. In this study, we present cryoelectron ...Plant high-affinity K transporters (HKTs) mediate Na and K uptake, maintain Na/K homeostasis, and therefore play crucial roles in plant salt tolerance. In this study, we present cryoelectron microscopy structures of HKTs from two classes, class I HKT1;1 from Arabidopsis thaliana (AtHKT1;1) and class II HKT2;1 from Triticum aestivum (TaHKT2;1), in both Na- and K-bound states at 2.6- to 3.0-Å resolutions. Both AtHKT1;1 and TaHKT2;1 function as homodimers. Each HKT subunit consists of four tandem domain units (D1-D4) with a repeated K-channel-like M-P-M topology. In each subunit, D1-D4 assemble into an ion conduction pore with a pseudo-four-fold symmetry. Although both TaHKT2;1 and AtHKT1;1 have only one putative Na ion bound in the selectivity filter with a similar coordination pattern, the two HKTs display different K binding modes in the filter. TaHKT2;1 has three K ions bound in the selectivity filter, but AtHKT1;1 has only two K ions bound in the filter, which has a narrowed external entrance due to the presence of a Ser residue in the first filter motif. These structures, along with computational, mutational, and electrophysiological analyses, enable us to pinpoint key residues that are critical for the ion selectivity of HKTs. The findings provide new insights into the ion selectivity and ion transport mechanisms of plant HKTs and improve our understanding about how HKTs mediate plant salt tolerance and enhance crop growth. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8w9v.cif.gz | 174.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8w9v.ent.gz | 134.6 KB | Display | PDB format |
PDBx/mmJSON format | 8w9v.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8w9v_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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Full document | 8w9v_full_validation.pdf.gz | 1.2 MB | Display | |
Data in XML | 8w9v_validation.xml.gz | 32 KB | Display | |
Data in CIF | 8w9v_validation.cif.gz | 46.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/w9/8w9v ftp://data.pdbj.org/pub/pdb/validation_reports/w9/8w9v | HTTPS FTP |
-Related structure data
Related structure data | 37382MC 8w9nC 8w9oC 8w9tC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 60200.590 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Triticum aestivum (bread wheat) / Production host: Homo sapiens (human) / References: UniProt: A0A3B6RK40 #2: Chemical | ChemComp-K / Has ligand of interest | 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 |
-Sample preparation
Component | Name: structure of TaHKT2;1 in KCl at 2.9 Angstroms resolution Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT |
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Source (natural) | Organism: Arabidopsis thaliana (thale cress) |
Source (recombinant) | Organism: Homo sapiens (human) / Cell: HEK 293 |
Buffer solution | pH: 8 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-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: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1600 nm / Nominal defocus min: 800 nm / Cs: 2.7 mm |
Image recording | Average exposure time: 8 sec. / Electron dose: 52 e/Å2 / Film or detector model: GATAN K2 QUANTUM (4k x 4k) |
-Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
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3D reconstruction | Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 73064 / Symmetry type: POINT | ||||||||||||||||||||||||
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