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- PDB-9is8: Cryo-EM structure of AKT1-AtKC1(G315D) -

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Basic information

Entry
Database: PDB / ID: 9is8
TitleCryo-EM structure of AKT1-AtKC1(G315D)
Components
  • Potassium channel AKT1
  • Potassium channel KAT3
KeywordsMEMBRANE PROTEIN / VGIC / Plant Channel
Function / homology
Function and homology information


root hair elongation / regulation of stomatal closure / response to water deprivation / inward rectifier potassium channel activity / response to nematode / potassium ion import across plasma membrane / voltage-gated potassium channel activity / monoatomic ion channel complex / response to salt stress / potassium ion transmembrane transport ...root hair elongation / regulation of stomatal closure / response to water deprivation / inward rectifier potassium channel activity / response to nematode / potassium ion import across plasma membrane / voltage-gated potassium channel activity / monoatomic ion channel complex / response to salt stress / potassium ion transmembrane transport / potassium ion transport / endoplasmic reticulum / identical protein binding / plasma membrane
Similarity search - Function
Potassium channel KAT/AKT / KHA domain / KHA, dimerisation domain of potassium ion channel / KHA domain profile. / Potassium channel, voltage-dependent, EAG/ELK/ERG / Cyclic nucleotide-monophosphate binding domain / Cyclic nucleotide-binding domain / cAMP/cGMP binding motif profile. / Cyclic nucleotide-binding domain / Cyclic nucleotide-binding domain superfamily ...Potassium channel KAT/AKT / KHA domain / KHA, dimerisation domain of potassium ion channel / KHA domain profile. / Potassium channel, voltage-dependent, EAG/ELK/ERG / Cyclic nucleotide-monophosphate binding domain / Cyclic nucleotide-binding domain / cAMP/cGMP binding motif profile. / Cyclic nucleotide-binding domain / Cyclic nucleotide-binding domain superfamily / RmlC-like jelly roll fold / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Ion transport domain / Ion transport protein
Similarity search - Domain/homology
: / Chem-POV / Potassium channel KAT3 / Potassium channel AKT1
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.77 Å
AuthorsDongliang, L. / Zijie, Z. / Yannan, Q. / Yuyue, T. / Huaizong, S.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: Plant Commun / Year: 2025
Title: AtKC1 inhibits AKT1 activation via its amino-terminal inhibitory domain.
Authors: Zijie Zheng / Yannan Qu / Jiexin Chen / Yuyue Tang / Dongliang Liu / Zhuo Huang / Huaizong Shen /
History
DepositionJul 17, 2024Deposition site: PDBJ / Processing site: PDBC
Revision 1.0May 21, 2025Provider: repository / Type: Initial release
Revision 1.1May 28, 2025Group: Data collection / Database references / Category: citation / em_admin / Item: _citation.journal_volume / _em_admin.last_update

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Potassium channel AKT1
B: Potassium channel KAT3
C: Potassium channel AKT1
D: Potassium channel AKT1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)382,98911
Polymers379,8324
Non-polymers3,1587
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein Potassium channel AKT1


Mass: 99812.266 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: AKT1, At2g26650, F18A8.2 / Production host: Homo sapiens (human) / References: UniProt: Q38998
#2: Protein Potassium channel KAT3 / AKT4 / AtKC1 / Potassium channel TKC


Mass: 80394.922 Da / Num. of mol.: 1 / Mutation: G315D
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: KAT3, AKT4, KC1, At4g32650, F4D11.150 / Production host: Homo sapiens (human) / References: UniProt: P92960
#3: Chemical
ChemComp-POV / (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / POPC


Mass: 760.076 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C42H82NO8P / Comment: phospholipid*YM
#4: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: K
Has ligand of interestN
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Complex of AKT1 and AtKC1(G315D) / Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT
Source (natural)Organism: Arabidopsis thaliana (thale cress)
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 1800 nm / Nominal defocus min: 1200 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 2.77 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 649659 / Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00815018
ELECTRON MICROSCOPYf_angle_d0.70220389
ELECTRON MICROSCOPYf_dihedral_angle_d31.9961990
ELECTRON MICROSCOPYf_chiral_restr0.0482305
ELECTRON MICROSCOPYf_plane_restr0.0042551

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