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- EMDB-35768: ABCG25 Wild Type in Apo-state -

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Basic information

Entry
Database: EMDB / ID: EMD-35768
TitleABCG25 Wild Type in Apo-state
Map data
Sample
  • Organelle or cellular component: ABCG25 from Arabidopsis thaliana
    • Protein or peptide: ABC transporter G family member 25
KeywordsABA / ABCG / plant hormone / TRANSPORT PROTEIN
Function / homologyProtein of unknown function DUF1425 / YcfL-like superfamily / Protein of unknown function (DUF1425) / Prokaryotic membrane lipoprotein lipid attachment site profile. / DUF1425 domain-containing protein
Function and homology information
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-
UpdateOct 23, 2024-
Current statusOct 23, 2024Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_35768.png

Downloads & links

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Map

FileDownload / File: emd_35768.map.gz / Format: CCP4 / Size: 52.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

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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 (log scale)
Contour LevelBy AUTHOR: 0.7
Minimum - Maximum-3.4277244 - 6.500223
Average (Standard dev.)0.012694557 (±0.14051345)
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: half map 1

Fileemd_35768_half_map_1.map
Annotationhalf map 1
Projections & Slices
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Half map: half map 2

Fileemd_35768_half_map_2.map
Annotationhalf map 2
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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

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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: all
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: 72.983867 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 VLDEPTSGLD 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: DUF1425 domain-containing protein

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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: 174479
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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