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- EMDB-35774: ABCG25 EQ mutant in ATP-bound state -

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Basic information

Entry
Database: EMDB / ID: EMD-35774
TitleABCG25 EQ mutant in ATP-bound state
Map data
Sample
  • Organelle or cellular component: ABCG25 from Arabidopsis thaliana
    • Protein or peptide: ABC transporter G family member 25
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION
KeywordsABA / ABCG / plant hormone / TRANSPORT PROTEIN
Function / homology
Function and homology information


intercellular transport / negative regulation of post-embryonic development / abscisic acid transport / export from cell / response to abscisic acid / abscisic acid-activated signaling pathway / efflux transmembrane transporter activity / ATPase-coupled transmembrane transporter activity / ABC-type transporter activity / response to cold ...intercellular transport / negative regulation of post-embryonic development / abscisic acid transport / export from cell / response to abscisic acid / abscisic acid-activated signaling pathway / efflux transmembrane transporter activity / ATPase-coupled transmembrane transporter activity / ABC-type transporter activity / response to cold / transmembrane transport / response to heat / ATP hydrolysis activity / ATP binding / plasma membrane
Similarity search - Function
ABC transporter family G domain / ABC-2 type transporter / : / ABC-2 type transporter / ABC-2 type transporter / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ABC transporter G family member 25
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.0 Å
AuthorsSun L / Liu X / Ying W / Liao L / Wei H
Funding support China, 1 items
OrganizationGrant numberCountry
Chinese Academy of SciencesXDB37020103 China
CitationJournal: Nat Plants / Year: 2023
Title: Structural basis for abscisic acid efflux mediated by ABCG25 in Arabidopsis thaliana.
Authors: Wei Ying / Lianghuan Liao / Hong Wei / Yongxiang Gao / Xin Liu / Linfeng Sun /
Abstract: Abscisic acid (ABA) is a phytohormone essential to the regulation of numerous aspects of plant growth and development. The cellular level of ABA is critical to its signalling and is determined by its ...Abscisic acid (ABA) is a phytohormone essential to the regulation of numerous aspects of plant growth and development. The cellular level of ABA is critical to its signalling and is determined by its rate of biosynthesis, catabolism and the rates of ABA transport. ABCG25 in Arabidopsis thaliana has been identified to be an ABA exporter and play roles in regulating stomatal closure and seed germination. However, its ABA transport mechanism remains unknown. Here we report the structures of ABCG25 under different states using cryo-electron microscopy single particle analysis: the apo state and ABA-bound state of the wild-type ABCG25 and the ATP-bound state of the ATPase catalytic mutant. ABCG25 forms a homodimer. ABA binds to a cone-shaped, cytosolic-facing cavity formed in the middle of the transmembrane domains. Key residues in ABA binding are identified and verified by a cell-based ABA transport assay. ATP binding leads to closing of the nucleotide-binding domains of opposing monomers and conformational transitions of the transmembrane domains. Together, these results provide insights into the substrate recognition and transport mechanisms of ABCG25 in Arabidopsis, and facilitate our understanding of the ABA transport and signalling pathway in plants.
History
DepositionMar 30, 2023-
Header (metadata) releaseApr 10, 2024-
Map releaseApr 10, 2024-
UpdateNov 13, 2024-
Current statusNov 13, 2024Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_35774.png

Downloads & links

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Map

FileDownload / File: emd_35774.map.gz / Format: CCP4 / Size: 52.7 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.)
1.1 Å/pix.
x 240 pix.
= 264. Å		1.1 Å/pix.
x 240 pix.
= 264. Å		1.1 Å/pix.
x 240 pix.
= 264. Å

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.1 Å
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Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.6
Minimum - Maximum-3.8137708 - 7.0401673
Average (Standard dev.)0.003692074 (±0.14675735)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions240240240
Spacing240240240
CellA=B=C: 264.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_35774_half_map_1.map
Projections & Slices
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Half map: #2

Fileemd_35774_half_map_2.map
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Sample components

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Entire : ABCG25 from Arabidopsis thaliana

EntireName: ABCG25 from Arabidopsis thaliana
Components
  • Organelle or cellular component: ABCG25 from Arabidopsis thaliana
    • Protein or peptide: ABC transporter G family member 25
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION

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Supramolecule #1: ABCG25 from Arabidopsis thaliana

SupramoleculeName: ABCG25 from Arabidopsis thaliana / 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: ABC transporter G family member 25

MacromoleculeName: ABC transporter G family member 25 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Arabidopsis thaliana (thale cress)
Molecular weightTheoretical: 72.982883 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MSAFDGVENQ MNGPDSSPRL SQDPREPRSL LSSSCFPITL KFVDVCYRVK IHGMSNDSCN IKKLLGLKQK PSDETRSTEE RTILSGVTG MISPGEFMAV LGPSGSGKST LLNAVAGRLH GSNLTGKILI NDGKITKQTL KRTGFVAQDD LLYPHLTVRE T LVFVALLR ...String:
MSAFDGVENQ MNGPDSSPRL SQDPREPRSL LSSSCFPITL KFVDVCYRVK IHGMSNDSCN IKKLLGLKQK PSDETRSTEE RTILSGVTG MISPGEFMAV LGPSGSGKST LLNAVAGRLH GSNLTGKILI NDGKITKQTL KRTGFVAQDD LLYPHLTVRE T LVFVALLR LPRSLTRDVK LRAAESVISE LGLTKCENTV VGNTFIRGIS GGERKRVSIA HELLINPSLL VLDQPTSGLD AT AALRLVQ TLAGLAHGKG KTVVTSIHQP SSRVFQMFDT VLLLSEGKCL FVGKGRDAMA YFESVGFSPA FPMNPADFLL DLA NGVCQT DGVTEREKPN VRQTLVTAYD TLLAPQVKTC IEVSHFPQDN ARFVKTRVNG GGITTCIATW FSQLCILLHR LLKE RRHES FDLLRIFQVV AASILCGLMW WHSDYRDVHD RLGLLFFISI FWGVLPSFNA VFTFPQERAI FTRERASGMY TLSSY FMAH VLGSLSMELV LPASFLTFTY WMVYLRPGIV PFLLTLSVLL LYVLASQGLG LALGAAIMDA KKASTIVTVT MLAFVL TGG YYVNKVPSGM VWMKYVSTTF YCYRLLVAIQ YGSGEEILRM LGCDSKGKQG ASAATSAGCR FVEEEVIGDV GMWTSVG VL FLMFFGYRVL AYLALRRIKH

UniProtKB: ABC transporter G family member 25

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Macromolecule #2: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 2 / Number of copies: 2 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

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Macromolecule #3: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 3 / Number of copies: 2 / Formula: MG
Molecular weightTheoretical: 24.305 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: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (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: DIFFRACTION / Nominal defocus max: 2.3000000000000003 µm / Nominal defocus min: 1.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 408077
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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