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- EMDB-27307: E. coli ATP synthase imaged in 10mM MgATP State2 "down" Fo classified -

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Basic information

Entry
Database: EMDB / ID: EMD-27307
TitleE. coli ATP synthase imaged in 10mM MgATP State2 "down" Fo classified
Map data
Sample
  • Complex: ATP synthase
    • Protein or peptide: x 8 types
  • Ligand: x 3 types
KeywordsEnergy / ATP hyrolysis / ATP synthesis / Motor / Membrane protein / cryoEM
Function / homology
Function and homology information


proton motive force-driven plasma membrane ATP synthesis / proton-transporting ATP synthase complex, coupling factor F(o) / proton-transporting ATP synthase complex, catalytic core F(1) / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / hydrolase activity / 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 / ATPase, OSCP/delta subunit, conserved site ...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 / ATPase, OSCP/delta subunit, conserved site / ATP synthase delta (OSCP) subunit signature. / 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, 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, F1 complex, alpha subunit nucleotide-binding domain / 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 subunit beta / ATP synthase epsilon chain / ATP synthase subunit alpha / ATP synthase subunit a / ATP synthase gamma chain / ATP synthase subunit b / ATP synthase subunit c / ATP synthase subunit delta
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsSobti M / Stewart AG
Funding support Australia, 1 items
OrganizationGrant numberCountry
National Health and Medical Research Council (NHMRC, Australia) Australia
CitationJournal: Commun Biol / Year: 2023
Title: Changes within the central stalk of E. coli FF ATP synthase observed after addition of ATP.
Authors: Meghna Sobti / Yi C Zeng / James L Walshe / Simon H J Brown / Robert Ishmukhametov / Alastair G Stewart /
Abstract: FF ATP synthase functions as a biological generator and makes a major contribution to cellular energy production. Proton flow generates rotation in the F motor that is transferred to the F motor to ...FF ATP synthase functions as a biological generator and makes a major contribution to cellular energy production. Proton flow generates rotation in the F motor that is transferred to the F motor to catalyze ATP production, with flexible F/F coupling required for efficient catalysis. FF ATP synthase can also operate in reverse, hydrolyzing ATP and pumping protons, and in bacteria this function can be regulated by an inhibitory ε subunit. Here we present cryo-EM data showing E. coli FF ATP synthase in different rotational and inhibited sub-states, observed following incubation with 10 mM MgATP. Our structures demonstrate how structural transitions within the inhibitory ε subunit induce torsional movement in the central stalk, thereby enabling its rotation within the F motor. This highlights the importance of the central rotor for flexible coupling of the F and F motors and provides further insight into the regulatory mechanism mediated by subunit ε.
History
DepositionJun 14, 2022-
Header (metadata) releaseJan 25, 2023-
Map releaseJan 25, 2023-
UpdateJun 12, 2024-
Current statusJun 12, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_27307.png

Downloads & links

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Map

FileDownload / File: emd_27307.map.gz / Format: CCP4 / Size: 166.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.08 Å/pix.
x 352 pix.
= 379.808 Å		1.08 Å/pix.
x 352 pix.
= 379.808 Å		1.08 Å/pix.
x 352 pix.
= 379.808 Å

Surface

Projections

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.079 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.01
Minimum - Maximum-0.021473767 - 0.06074541
Average (Standard dev.)-0.00013322075 (±0.0025266882)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions352352352
Spacing352352352
CellA=B=C: 379.80798 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_27307_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_27307_half_map_2.map
Projections & Slices
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Histogram (log scale)

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Sample components

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Entire : ATP synthase

EntireName: ATP synthase
Components
  • Complex: ATP synthase
    • 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

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Supramolecule #1: ATP synthase

SupramoleculeName: ATP synthase / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#8
Source (natural)Organism: Escherichia coli (E. coli)

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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: Escherichia coli (E. coli)
Molecular weightTheoretical: 55.153609 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MQLNSTEISE LIKQRIAQFN VVSEAHNEGT IVSVSDGVIR IHGLADAMQG EMISLPGNRY AIALNLERDS VGAVVMGPYA DLAEGMKVK ATGRILEVPV GRGLLGRVVN TLGAPIDGKG PLDHDGFSAV EAIAPGVIER QSVDQPVQTG YKAVDSMIPI G RGQRELII ...String:
MQLNSTEISE LIKQRIAQFN VVSEAHNEGT IVSVSDGVIR IHGLADAMQG EMISLPGNRY AIALNLERDS VGAVVMGPYA DLAEGMKVK ATGRILEVPV GRGLLGRVVN TLGAPIDGKG PLDHDGFSAV EAIAPGVIER QSVDQPVQTG YKAVDSMIPI G RGQRELII GDRQTGKTAL AIDAIINQRD SGIKAIYVAI GQKASTISNV VRKLEEHGAL ANTIVVVATA SESAALQYLA PY AGAAMGE YFRDRGEDAL IIYDDLSKQA VAYRQISLLL RRPPGREAFP GDVFYLHSRL LERAARVNAE YVEAFTKGEV KGK TGSLTA LPIIETQAGD VSAFVPTNVI SITDGQIFLE TNLFNAGIRP AVNPGISVSR VGGAAQTKIM KKLSGGIRTA LAQY RELAA FSQFASDLDD ATRKQLDHGQ KVTELLKQKQ YAPMSVAQQS LVLFAAERGY LADVELSKIG SFEAALLAYV DRDHA PLMQ EINQTGGYND EIEGKLKGIL DSFKATQSW

UniProtKB: ATP synthase subunit alpha

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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: Escherichia coli (E. coli)
Molecular weightTheoretical: 50.346129 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MATGKIVQVI GAVVDVEFPQ DAVPRVYDAL EVQNGNERLV LEVQQQLGGG IVRTIAMGSS DGLRRGLDVK DLEHPIEVPV GKATLGRIM NVLGEPVDMK GEIGEEERWA IHRAAPSYEE LSNSQELLET GIKVIDLMAP FAKGGKVGLF GGAGVGKTVN M MELIRNIA ...String:
MATGKIVQVI GAVVDVEFPQ DAVPRVYDAL EVQNGNERLV LEVQQQLGGG IVRTIAMGSS DGLRRGLDVK DLEHPIEVPV GKATLGRIM NVLGEPVDMK GEIGEEERWA IHRAAPSYEE LSNSQELLET GIKVIDLMAP FAKGGKVGLF GGAGVGKTVN M MELIRNIA IEHSGYSVFA GVGERTREGN DFYHEMTDSN VIDKVSLVYG QMNEPPGNRL RVALTGLTMA EKFRDEGRDV LL FVDNIYR YTLAGTEVSA LLGRMPSAVG YQPTLAEEMG VLQERITSTK TGSITSVQAV YVPADDLTDP SPATTFAHLD ATV VLSRQI ASLGIYPAVD PLDSTSRQLD PLVVGQEHYD TARGVQSILQ RYQELKDIIA ILGMDELSEE DKLVVARARK IQRF LSQPF FVAEVFTGSP GKYVSLKDTI RGFKGIMEGE YDHLPEQAFY MVGSIEEAVE KAKKL

UniProtKB: ATP synthase subunit beta

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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: Escherichia coli (E. coli)
Molecular weightTheoretical: 31.539285 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MAGAKDIRSK IASVQNTQKI TKAMEMVAAS KMRKSQDRMA ASRPYAETMR KVIGHLAHGN LEYKHPYLED RDVKRVGYLV VSTDRGLAG GLNINLFKKL LAEMKTWTDK GVQADLAMIG SKGVSFFNSV GGNVVAQVTG MGDNPSLSEL IGPVKVMLQA Y DEGRLDKL ...String:
MAGAKDIRSK IASVQNTQKI TKAMEMVAAS KMRKSQDRMA ASRPYAETMR KVIGHLAHGN LEYKHPYLED RDVKRVGYLV VSTDRGLAG GLNINLFKKL LAEMKTWTDK GVQADLAMIG SKGVSFFNSV GGNVVAQVTG MGDNPSLSEL IGPVKVMLQA Y DEGRLDKL YIVSNKFINT MSQVPTISQL LPLPASDDDD LKHKSWDYLY EPDPKALLDT LLRRYVESQV YQGVVENLAS EQ AARMVAM KAATDNGGSL IKELQLVYNK ARQASITQEL TEIVSGAAAV

UniProtKB: ATP synthase gamma chain

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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: Escherichia coli (E. coli)
Molecular weightTheoretical: 15.087244 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MAMTYHLDVV SAEQQMFSGL VEKIQVTGSE GELGIYPGHA PLLTAIKPGM IRIVKQHGHE EFIYLSGGIL EVQPGNVTVL ADTAIRGQD LDEARAMEAK RKAEEHISSS HGDVDYAQAS AELAKAIAQL RVIELTKKAM

UniProtKB: ATP synthase epsilon chain

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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: Escherichia coli (E. coli)
Molecular weightTheoretical: 8.259064 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MENLNMDLLY MAAAVMMGLA AIGAAIGIGI LGGKFLEGAA RQPDLIPLLR TQFFIVMGLV DAIPMIAVGL GLYVMFAVA

UniProtKB: ATP synthase subunit c

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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: Escherichia coli (E. coli)
Molecular weightTheoretical: 19.289061 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MSEFITVARP YAKAAFDFAV EHQSVERWQD MLAFAAEVTK NEQMAELLSG ALAPETLAES FIAVAGEQLD ENGQNLIRVM AENGRLNAL PDVLEQFIHL RAVSEATAEV DVISAAALSE QQLAKISAAM EKRLSRKVKL NAKIDKSVMA GVIIRAGDMV I DGSVRGRL ERLADVLQS

UniProtKB: ATP synthase subunit delta

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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: Escherichia coli (E. coli)
Molecular weightTheoretical: 17.289953 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MNLNATILGQ AIAFVLFVLF CMKYVWPPLM AAIEKRQKEI ADGLASAERA HKDLDLAKAS ATDQLKKAKA EAQVIIEQAN KRRSQILDE AKAEAEQERT KIVAQAQAEI EAERKRAREE LRKQVAILAV AGAEKIIERS VDEAANSDIV DKLVAEL

UniProtKB: ATP synthase subunit b

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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: Escherichia coli (E. coli)
Molecular weightTheoretical: 30.324096 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MASENMTPQD YIGHHLNNLQ LDLRTFSLVD PQNPPATFWT INIDSMFFSV VLGLLFLVLF RSVAKKATSG VPGKFQTAIE LVIGFVNGS VKDMYHGKSK LIAPLALTIF VWVFLMNLMD LLPIDLLPYI AEHVLGLPAL RVVPSADVNV TLSMALGVFI L ILFYSIKM ...String:
MASENMTPQD YIGHHLNNLQ LDLRTFSLVD PQNPPATFWT INIDSMFFSV VLGLLFLVLF RSVAKKATSG VPGKFQTAIE LVIGFVNGS VKDMYHGKSK LIAPLALTIF VWVFLMNLMD LLPIDLLPYI AEHVLGLPAL RVVPSADVNV TLSMALGVFI L ILFYSIKM KGIGGFTKEL TLQPFNHWAF IPVNLILEGV SLLSKPVSLG LRLFGNMYAG ELIFILIAGL LPWWSQWILN VP WAIFHIL IITLQAFIFM VLTIVYLSMA SEEH

UniProtKB: ATP synthase subunit a

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Macromolecule #9: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 9 / Number of copies: 4 / 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 #10: MAGNESIUM ION

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

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Macromolecule #11: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 11 / Number of copies: 2 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

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

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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: 7.5
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: 48.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.8 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: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 40510
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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