[English] 日本語
Yorodumi
- EMDB-70000: Pseudomonas aeruginosa ATPase State1 F1Fo focused -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-70000
TitlePseudomonas aeruginosa ATPase State1 F1Fo focused
Map dataPseudomonas aeruginosa ATPase State1 F1Fo focused
Sample
  • Complex: Pseudomonas aeruginosa ATPase
    • Protein or peptide: x 8 types
  • Ligand: x 4 types
KeywordsATPase / electron transport / energy
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 / H+-transporting two-sector ATPase / proton-transporting ATP synthase complex / proton-transporting ATP synthase activity, rotational mechanism / ADP binding / lipid binding / ATP hydrolysis activity / ATP binding / plasma membrane
Similarity search - Function
ATP synthase delta/epsilon subunit, C-terminal domain / ATP synthase, Delta/Epsilon chain, long alpha-helix domain / 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 delta/epsilon subunit, C-terminal domain superfamily / ATP synthase, F0 complex, subunit C, bacterial/chloroplast ...ATP synthase delta/epsilon subunit, C-terminal domain / ATP synthase, Delta/Epsilon chain, long alpha-helix domain / 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 delta/epsilon subunit, C-terminal domain superfamily / ATP synthase, F0 complex, subunit C, bacterial/chloroplast / F1F0 ATP synthase OSCP/delta subunit, N-terminal domain superfamily / 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. / ATPase, OSCP/delta subunit / ATP synthase delta (OSCP) subunit / ATP synthase, F1 complex, delta/epsilon subunit / ATP synthase, F1 complex, delta/epsilon subunit, N-terminal / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase, Delta/Epsilon chain, beta-sandwich domain / 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. / ATP synthase, F1 complex, gamma subunit conserved site / ATP synthase gamma subunit signature. / ATP synthase, F1 complex, beta subunit / ATP synthase, alpha subunit, C-terminal domain superfamily / : / ATP synthase, F1 complex, alpha subunit nucleotide-binding domain / ATP synthase, F1 complex, gamma subunit / ATP synthase, F1 complex, gamma subunit superfamily / ATP synthase / ATP synthase, alpha subunit, C-terminal / ATP synthase, F1 complex, alpha subunit / ATP synthase alpha/beta chain, C terminal domain / V-ATPase proteolipid subunit C-like domain / F/V-ATP synthase subunit C superfamily / ATP synthase subunit C / : / ATPase, F1/V1 complex, beta/alpha subunit, C-terminal / C-terminal domain of V and A type ATP synthase / ATP synthase subunit alpha, N-terminal domain-like superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain / ATP synthase alpha/beta family, beta-barrel domain / ATPase, alpha/beta subunit, nucleotide-binding domain, active site / ATP synthase alpha and beta subunits signature. / ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain / ATP synthase alpha/beta family, nucleotide-binding domain / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ATP synthase epsilon chain / ATP synthase subunit beta / ATP synthase gamma chain / ATP synthase subunit alpha / ATP synthase subunit delta / 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: 2.77 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

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_70000.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationPseudomonas aeruginosa ATPase State1 F1Fo 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: 0.06
Minimum - Maximum-0.121622905 - 0.35004997
Average (Standard dev.)0.0018444486 (±0.012092375)
SymmetrySpace group: 1
Details

EMDB XML:

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

-
Supplemental data

-
Half map: Half Map A

Fileemd_70000_half_map_1.map
AnnotationHalf Map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: Half Map B

Fileemd_70000_half_map_2.map
AnnotationHalf Map B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

+
Entire : Pseudomonas aeruginosa ATPase

EntireName: Pseudomonas aeruginosa ATPase
Components
  • Complex: Pseudomonas aeruginosa ATPase
    • Protein or peptide: ATP synthase subunit alpha
    • Protein or peptide: ATP synthase subunit beta
    • Protein or peptide: ATP synthase gamma chain
    • Protein or peptide: ATP synthase epsilon chain
    • Protein or peptide: ATP synthase subunit c
    • Protein or peptide: ATP synthase subunit delta
    • Protein or peptide: ATP synthase subunit b
    • Protein or peptide: ATP synthase subunit a
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: ZINC ION

+
Supramolecule #1: Pseudomonas aeruginosa ATPase

SupramoleculeName: Pseudomonas aeruginosa ATPase / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#8
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)

+
Macromolecule #1: ATP synthase subunit alpha

MacromoleculeName: ATP synthase subunit alpha / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO / EC number: H+-transporting two-sector ATPase
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)
Molecular weightTheoretical: 55.264785 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MQQLNPSEIS EIIKGRIEKL DVASQARNEG TIVSVSDGIV RIYGLADVMY GEMIEFPGGV YGMALNLEQD SVGAVVLGEY QGLAEGMNA KCTGRILEVP VGPELLGRVV DALGNPIDGK GPIDAKATDA VEKVAPGVIW RKSVDQPVQT GYKSVDAMIP V GRGQRELI ...String:
MQQLNPSEIS EIIKGRIEKL DVASQARNEG TIVSVSDGIV RIYGLADVMY GEMIEFPGGV YGMALNLEQD SVGAVVLGEY QGLAEGMNA KCTGRILEVP VGPELLGRVV DALGNPIDGK GPIDAKATDA VEKVAPGVIW RKSVDQPVQT GYKSVDAMIP V GRGQRELI IGDRQIGKTA LAVDAIINQK DSGIKCVYVA IGQKQSTIAN VVRKLEENGA LANTIVVAAS ASESAALQYL AP YSGCTMG EYFRDRGEDA LIVYDDLSKQ AVAYRQISLL LRRPPGREAY PGDVFYLHSR LLERASRVSE EYVEKFTNGA VTG KTGSLT ALPIIETQAG DVSAFVPTNV ISITDGQIFL ESAMFNSGIR PAVNAGISVS RVGGAAQTKI IKKLSGGIRT ALAQ YRELA AFAQFASDLD EATRKQLEHG QRVTELMKQK QYAPMSIAEM SLSLYAAERG FLQDVEIAKV GSFEQALISY FQREH AALL AKINEKGDFN DEIDAGIKAG IEKFKATQT

UniProtKB: ATP synthase subunit alpha

+
Macromolecule #2: ATP synthase subunit beta

MacromoleculeName: ATP synthase subunit beta / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO / EC number: H+-transporting two-sector ATPase
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)
Molecular weightTheoretical: 50.380129 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MHHHHHHSSG RIVQIIGAVI DVEFPRDAVP SIYEALKVQG VETTLEVQQQ LGDGVVRSIA MGSTEGLKRG LNVDSTGAAI SVPVGKATL GRIMDVLGNP IDEAGPIGEE ERWGIHREAP SYADQAGGNE LLETGIKVID LVCPFAKGGK VGLFGGAGVG K TVNMMELI ...String:
MHHHHHHSSG RIVQIIGAVI DVEFPRDAVP SIYEALKVQG VETTLEVQQQ LGDGVVRSIA MGSTEGLKRG LNVDSTGAAI SVPVGKATL GRIMDVLGNP IDEAGPIGEE ERWGIHREAP SYADQAGGNE LLETGIKVID LVCPFAKGGK VGLFGGAGVG K TVNMMELI RNIAIEHSGY SVFAGVGERT REGNDFYHEM KDSNVLDKVA LVYGQMNEPP GNRLRVALTG LTMAEKFRDE GR DVLLFID NIYRYTLAGT EVSALLGRMP SAVGYQPTLA EEMGVLQERI TSTKKGSITS IQAVYVPADD LTDPSPATTF AHL DATVVL SRDIASLGIY PAVDPLDSTS RQLDPLVIGQ DHYDTARGVQ YVLQRYKELK DIIAILGMDE LSEADKLLVA RARK IQRFL SQPFFVAEVF TGSPGKYVSL KDTIAGFKGI LNGDYDHLPE QAFYMVGGIE EAVEKAKKL

UniProtKB: ATP synthase subunit beta

+
Macromolecule #3: ATP synthase gamma chain

MacromoleculeName: ATP synthase gamma chain / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)
Molecular weightTheoretical: 31.593328 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MAGAKEIRSK IASIKSTQKI TNAMEKVAVS KMRKAQMRMA AGRPYAERIR QVIGHLANAN PEYRHPFMVE REVKRVGYIV VSSDRGLCG GLNINLFKSL VKDMSGYREQ GAEIDLCVIG SKGASFFRSF GGNVVAAISH LGEEPSINDL IGSVKVMLDA Y LEGRIDRL ...String:
MAGAKEIRSK IASIKSTQKI TNAMEKVAVS KMRKAQMRMA AGRPYAERIR QVIGHLANAN PEYRHPFMVE REVKRVGYIV VSSDRGLCG GLNINLFKSL VKDMSGYREQ GAEIDLCVIG SKGASFFRSF GGNVVAAISH LGEEPSINDL IGSVKVMLDA Y LEGRIDRL FVVSNKFVNT MTQKPTVEQL IPLVADDDQE LKHHWDYLYE PDAKSLLDGL LVRYVESQVY QAVVENNACE QA ARMIAMK NATDNAGELI SDLQLIYNKA RQAAITQEIS EIVGGAAAV

UniProtKB: ATP synthase gamma chain

+
Macromolecule #4: ATP synthase epsilon chain

MacromoleculeName: ATP synthase epsilon chain / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)
Molecular weightTheoretical: 14.741866 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MAITVHCDIV SAEAEIFSGL VEMVIAHGAL GDLGIAPGHA PLITDLKPGP IRLVKQGGEQ EVYYISGGFL EVQPNMVKVL ADTVVRAGD LDEAAAQEAL KAAEKALQGK GAEFDYSAAA ARLAEAAAQL RTVQQLRKKF GG

UniProtKB: ATP synthase epsilon chain

+
Macromolecule #5: ATP synthase subunit c

MacromoleculeName: ATP synthase subunit c / type: protein_or_peptide / ID: 5 / 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

+
Macromolecule #6: ATP synthase subunit delta

MacromoleculeName: ATP synthase subunit delta / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)
Molecular weightTheoretical: 19.28398 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MAELTTLARP YAKAAFEYAQ AHQQLADWSA ALGVLAAVSQ DDTVRQLLKE PQLTSSAKAQ SLIDVCGDKL NAPAQNFVRT VAENKRLEL LPTIAEMYEQ LKAEQEKSVE VEVTSAFTLS KEQQDKLAKA LSARLSREVR LHASEDASLI GGVIIRAGDL V IDGSVRGK LAKLAEALKS

UniProtKB: ATP synthase subunit delta

+
Macromolecule #7: ATP synthase subunit b

MacromoleculeName: ATP synthase subunit b / type: protein_or_peptide / ID: 7 / 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

+
Macromolecule #8: ATP synthase subunit a

MacromoleculeName: ATP synthase subunit a / type: protein_or_peptide / ID: 8 / 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

+
Macromolecule #9: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 9 / Number of copies: 3 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

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

+
Macromolecule #10: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 10 / Number of copies: 5 / Formula: MG
Molecular weightTheoretical: 24.305 Da

+
Macromolecule #11: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 11 / Number of copies: 3 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

+
Macromolecule #12: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 12 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 62.0 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

+
Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.77 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 28761
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more