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- EMDB-62338: AtGORK Full length 1 -

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Basic information

Entry
Database: EMDB / ID: EMD-62338
TitleAtGORK Full length 1
Map data
Sample
  • Organelle or cellular component: AtGORK full length 1
    • Protein or peptide: Potassium channel GORK
  • Ligand: POTASSIUM ION
KeywordsComplex / TRANSPORT PROTEIN / PROTON TRANSPORT
Function / homology
Function and homology information


monoatomic ion transmembrane transporter activity / response to jasmonic acid / response to abscisic acid / response to water deprivation / outward rectifier potassium channel activity / monoatomic ion channel complex / monoatomic ion transport / response to cold / response to calcium ion / nucleus
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
Potassium channel GORK
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsChen YH / Li QY / Zhang CR / Tang LH
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: Protein Cell / Year: 2025
Title: Structural and mechanistic insights into symmetry conversion in plant GORK K+ channel regulation.
Authors: Qi-Yu Li / Li Qin / Ling-Hui Tang / Chun-Rui Zhang / Shouguang Huang / Ke Wang / Gao-Hua Zhang / Ning-Jie Hao / Qian Xiao / Tongxin Niu / Min Su / Rainer Hedrich / Yu-Hang Chen /
Abstract: GORK is a shaker-like potassium channel in plants that contains ankyrin (ANK) repeats. In guard cells, activation of GORK causes K+ efflux, reducing turgor pressure and closing stomata. However, how ...GORK is a shaker-like potassium channel in plants that contains ankyrin (ANK) repeats. In guard cells, activation of GORK causes K+ efflux, reducing turgor pressure and closing stomata. However, how GORK is regulated remains largely elusive. Here, we solved the cryo-EM structure of Arabidopsis GORK, revealing an unusual symmetry reduction (from C4 to C2) feature within its tetrameric assembly. This symmetry reduction in GORK channel is driven by ANK dimerization, which disrupts the coupling between transmembrane helices and cytoplasmic domains, thus maintaining GORK in an autoinhibited state. Electrophysiological and structural analyses further confirmed that ANK dimerization inhibits GORK, and its removal restores C4 symmetry, converting GORK to an activatable state. This dynamic switching between C2 and C4 symmetry, mediated by ANK dimerization, presents a GORK target site that guard cells regulate to switch the plant K+ channel between inhibited and activatable states, thus controlling stomatal movement in response to environmental stimuli.
History
DepositionNov 10, 2024-
Header (metadata) releaseOct 29, 2025-
Map releaseOct 29, 2025-
UpdateOct 29, 2025-
Current statusOct 29, 2025Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_62338.png

Downloads & links

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Map

FileDownload / File: emd_62338.map.gz / Format: CCP4 / Size: 91.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.06 Å/pix.
x 288 pix.
= 305.28 Å		1.06 Å/pix.
x 288 pix.
= 305.28 Å		1.06 Å/pix.
x 288 pix.
= 305.28 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.06 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0966
Minimum - Maximum-1.195031 - 1.8586965
Average (Standard dev.)0.00006463683 (±0.035738006)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions288288288
Spacing288288288
CellA=B=C: 305.27997 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_62338_half_map_1.map
Projections & Slices
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Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_62338_half_map_2.map
Projections & Slices
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Histogram (log scale)

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Sample components

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Entire : AtGORK full length 1

EntireName: AtGORK full length 1
Components
  • Organelle or cellular component: AtGORK full length 1
    • Protein or peptide: Potassium channel GORK
  • Ligand: POTASSIUM ION

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Supramolecule #1: AtGORK full length 1

SupramoleculeName: AtGORK full length 1 / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Arabidopsis thaliana (thale cress)

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Macromolecule #1: Potassium channel GORK

MacromoleculeName: Potassium channel GORK / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Arabidopsis thaliana (thale cress)
Molecular weightTheoretical: 87.653922 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: IHPKNRWYKA WEMFILVWAI YSSLFTPMEF GFFRGLPERL FVLDIVGQIA FLVDIVLQFF VAYRDTQTYR TVYKPTRIAF RYLKSHFLM DFIGCFPWDL IYKASGKHEL VRYLLWIRLF RVRKVVEFFQ RLEKDTRINY LFTRILKLLF VEVYCTHTAA C IFYYLATT ...String:
IHPKNRWYKA WEMFILVWAI YSSLFTPMEF GFFRGLPERL FVLDIVGQIA FLVDIVLQFF VAYRDTQTYR TVYKPTRIAF RYLKSHFLM DFIGCFPWDL IYKASGKHEL VRYLLWIRLF RVRKVVEFFQ RLEKDTRINY LFTRILKLLF VEVYCTHTAA C IFYYLATT LPPENEGYTW IGSLKLGDYS YENFREIDLW KRYTTALYFA IVTMATVGYG DIHAVNLREM IFVMIYVSFD MV LGAYLIG NITALIVKGS NTERFRDKMN DLISFMNRKK LGRDLRSQIT GHVRLQYDSH YTDTVMLQDI PASIRAKIAQ LLY LPYIKK VPLFKGCSTE FINQIVIRLH EEYFLPGEVI TEQGNVVDHL YFVCEGLLEA LVTKTDGSEE SVTLLGPHTS FGDI SIICN ISQPFTVRVC ELCHLLRLDK QSFSNILEIY FHDGRTILNN IMEEKESNDR IKKLESDIVI HIGKQEAELA LKVNS AAFQ GDFYQLKSLI RSGADPNKTD YDGRSPLHLA ACRGYEDITL FLIQEGVDVN LKDKFGHTPL FEAVKAGQEG VIGLLV KEG ASFNLEDSGN FLCTTVAKGD SDFLKRLLSS GMNPNSEDYD HRTPLHVAAS EGLFLMAKML VEAGASVISK DRWGNSP LD EARLCGNKKL IKLLEDVKNA QSSIYPSSLR ELQEERIERR KCTVFPFHPQ EAKEERSRKH GVVVWIPSNL EKLIVTAA K ELGLSDGASF VLLSEDQGRI TDIDMISDGH KLYMISDTTD QT

UniProtKB: Potassium channel GORK

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Macromolecule #2: POTASSIUM ION

MacromoleculeName: POTASSIUM ION / type: ligand / ID: 2 / Number of copies: 2 / Formula: K
Molecular weightTheoretical: 39.098 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 156313
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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