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- EMDB-70001: Pseudomonas aeruginosa ATPase State1 Fo focused -

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ID or keywords:

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Basic information

Entry
Database: EMDB / ID: EMD-70001
TitlePseudomonas aeruginosa ATPase State1 Fo focused
Map dataPseudomonas aeruginosa ATPase State1 Fo focused
Sample
  • Complex: Pseudomonas aeruginosa ATPase
    • Protein or peptide: ATP synthase subunit c
    • Protein or peptide: ATP synthase subunit b
    • Protein or peptide: ATP synthase subunit a
  • Ligand: ZINC ION
  • Ligand: water
KeywordsATPase / Cryo-EM / single particle / energy / ELECTRON TRANSPORT
Function / homology
Function and homology information


proton motive force-driven plasma membrane ATP synthesis / proton-transporting two-sector ATPase complex, proton-transporting domain / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase complex / proton-transporting ATP synthase activity, rotational mechanism / lipid binding / plasma membrane
Similarity search - Function
ATP synthase, F0 complex, subunit b, bacterial / F-type ATP synthase subunit B-like, membrane domain superfamily / : / ATP synthase, F0 complex, subunit A, bacterial/chloroplast / ATP synthase, F0 complex, subunit b/b', bacterial/chloroplast / ATP synthase B/B' CF(0) / ATP synthase, F0 complex, subunit C, bacterial/chloroplast / ATP synthase, F0 complex, subunit A / ATP synthase, F0 complex, subunit A, active site / ATP synthase, F0 complex, subunit A superfamily ...ATP synthase, F0 complex, subunit b, bacterial / F-type ATP synthase subunit B-like, membrane domain superfamily / : / ATP synthase, F0 complex, subunit A, bacterial/chloroplast / ATP synthase, F0 complex, subunit b/b', bacterial/chloroplast / ATP synthase B/B' CF(0) / ATP synthase, F0 complex, subunit C, bacterial/chloroplast / ATP synthase, F0 complex, subunit A / ATP synthase, F0 complex, subunit A, active site / ATP synthase, F0 complex, subunit A superfamily / ATP synthase A chain / ATP synthase a subunit signature. / ATP synthase, F0 complex, subunit C / F1F0 ATP synthase subunit C superfamily / ATP synthase, F0 complex, subunit C, DCCD-binding site / ATP synthase c subunit signature. / V-ATPase proteolipid subunit C-like domain / F/V-ATP synthase subunit C superfamily / ATP synthase subunit C
Similarity search - Domain/homology
ATP synthase subunit c / ATP synthase subunit a / ATP synthase subunit b
Similarity search - Component
Biological speciesPseudomonas aeruginosa (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.37 Å
AuthorsStewart AG / Sobti M
Funding support Australia, 1 items
OrganizationGrant numberCountry
National Health and Medical Research Council (NHMRC, Australia) Australia
CitationJournal: To Be Published
Title: Distinct Structural Features of Pseudomonas aeruginosa ATP Synthase Revealed by Cryo Electron Microscopy
Authors: Sobti M / Stewart AG
History
DepositionApr 3, 2025-
Header (metadata) releaseDec 10, 2025-
Map releaseDec 10, 2025-
UpdateDec 10, 2025-
Current statusDec 10, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_70001.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationPseudomonas aeruginosa ATPase State1 Fo focused
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 400 pix.
= 332. Å
0.83 Å/pix.
x 400 pix.
= 332. Å
0.83 Å/pix.
x 400 pix.
= 332. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.83 Å
Density
Contour LevelBy AUTHOR: 0.07
Minimum - Maximum-0.09205821 - 0.3083808
Average (Standard dev.)0.001751502 (±0.009930207)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 332.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Half Map B

Fileemd_70001_half_map_1.map
AnnotationHalf Map B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: Half Map A

Fileemd_70001_half_map_2.map
AnnotationHalf Map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : Pseudomonas aeruginosa ATPase

EntireName: Pseudomonas aeruginosa ATPase
Components
  • Complex: Pseudomonas aeruginosa ATPase
    • Protein or peptide: ATP synthase subunit c
    • Protein or peptide: ATP synthase subunit b
    • Protein or peptide: ATP synthase subunit a
  • Ligand: ZINC ION
  • Ligand: water

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Supramolecule #1: Pseudomonas aeruginosa ATPase

SupramoleculeName: Pseudomonas aeruginosa ATPase / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)

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Macromolecule #1: ATP synthase subunit c

MacromoleculeName: ATP synthase subunit c / type: protein_or_peptide / ID: 1 / Number of copies: 10 / Enantiomer: LEVO
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)
Molecular weightTheoretical: 8.61138 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
METVVGLTAI AVALLIGLGA LGTAIGFGLL GGKFLEGAAR QPEMVPMLQV KMFIVAGLLD AVTMIGVGIA LFFTFANPFV GQIAG

UniProtKB: ATP synthase subunit c

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Macromolecule #2: ATP synthase subunit b

MacromoleculeName: ATP synthase subunit b / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)
Molecular weightTheoretical: 16.978346 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MNINATLIGQ SVAFFIFVLF CMKFVWPPVI AALQERQKKI ADGLDAANRA ARDLELAHEK AGQQLREAKA QAAEIVEQAK KRANQIVDE ARDQARTEGE RLKAQAQAEI EQELNSVKDA LRAQVGALAV TGAEKILGAS IDANAHEQLV SKLAAEI

UniProtKB: ATP synthase subunit b

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Macromolecule #3: ATP synthase subunit a

MacromoleculeName: ATP synthase subunit a / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)
Molecular weightTheoretical: 31.944635 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MAAETASGYI QHHLQNLTFG RLPNGDWGFA HTAEQAKEMG FWAFHVDTLG WSVLLGVVFL FIFRLAAKKA TSGQPGGLQN FVEVMVEFV DTSVKDTFHG RNPLIAPLAL TVFVWIFLLN LIDLVPVDYL PMLAAKITGD EHLFFRAVAT TDPNATLGLS I SVFALIVF ...String:
MAAETASGYI QHHLQNLTFG RLPNGDWGFA HTAEQAKEMG FWAFHVDTLG WSVLLGVVFL FIFRLAAKKA TSGQPGGLQN FVEVMVEFV DTSVKDTFHG RNPLIAPLAL TVFVWIFLLN LIDLVPVDYL PMLAAKITGD EHLFFRAVAT TDPNATLGLS I SVFALIVF YSIKVKGIGG FLGELTLHPF SSKNIVVQIL LIPVNFLLEF VTLIAKPVSL ALRLFGNMYA GELIFILIAV MF GSGMFLL SALGVALNWA WAVFHILIIT LQAFIFMMLT IVYLSMAHED NH

UniProtKB: ATP synthase subunit a

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Macromolecule #4: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 4 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #5: water

MacromoleculeName: water / type: ligand / ID: 5 / Number of copies: 5 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER

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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 / Chamber humidity: 100 %

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 65.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.5 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: 2.37 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 143285
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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