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- EMDB-10573: Ovine ATP synthase 1a state -

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Basic information

Entry
Database: EMDB / ID: EMD-10573
TitleOvine ATP synthase 1a state
Map dataComposite map of state 1a of ovine F1Fo, obtained from series of focused refinements as described in the paper.
Sample
  • Complex: Purified ATP synthase from sheep heart mitochondria
    • Protein or peptide: x 17 types
  • Ligand: x 6 types
Function / homology
Function and homology information


negative regulation of cell adhesion involved in substrate-bound cell migration / ATP biosynthetic process / angiostatin binding / Formation of ATP by chemiosmotic coupling / Cristae formation / mitochondrial proton-transporting ATP synthase complex assembly / cellular response to interleukin-7 / mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) / mitochondrial proton-transporting ATP synthase complex / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) ...negative regulation of cell adhesion involved in substrate-bound cell migration / ATP biosynthetic process / angiostatin binding / Formation of ATP by chemiosmotic coupling / Cristae formation / mitochondrial proton-transporting ATP synthase complex assembly / cellular response to interleukin-7 / mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) / mitochondrial proton-transporting ATP synthase complex / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) / mitochondrial nucleoid / proton motive force-driven mitochondrial ATP synthesis / proton-transporting ATP synthase complex, coupling factor F(o) / proton motive force-driven ATP synthesis / proton transmembrane transporter activity / proton-transporting ATP synthase complex, catalytic core F(1) / positive regulation of blood vessel endothelial cell migration / MHC class I protein binding / aerobic respiration / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton transmembrane transport / proton-transporting ATP synthase activity, rotational mechanism / regulation of intracellular pH / lipid metabolic process / angiogenesis / mitochondrial inner membrane / lipid binding / cell surface / mitochondrion / ATP binding / plasma membrane
Similarity search - Function
ATP synthase membrane subunit K / ATP synthase regulation / ATP synthase, F0 complex, subunit G, mitochondrial / ATP synthase, F0 complex, subunit E, mitochondrial / ATP synthase subunit ATP5MJ, mitochondrial / Mitochondrial ATP synthase subunit g, animal / Mitochondrial ATP synthase g subunit / ATP synthase E chain / Mitochondrial proteolipid / ATP synthase protein 8, metazoa ...ATP synthase membrane subunit K / ATP synthase regulation / ATP synthase, F0 complex, subunit G, mitochondrial / ATP synthase, F0 complex, subunit E, mitochondrial / ATP synthase subunit ATP5MJ, mitochondrial / Mitochondrial ATP synthase subunit g, animal / Mitochondrial ATP synthase g subunit / ATP synthase E chain / Mitochondrial proteolipid / ATP synthase protein 8, metazoa / Mitochondrial F1-F0 ATP synthase subunit F, predicted / ATP synthase protein 8, mammals / ATP synthase protein 8 / Mitochondrial F1F0-ATP synthase, subunit f / ATP synthase-coupling factor 6, mitochondrial / ATP synthase-coupling factor 6 superfamily, mitochondrial / Mitochondrial ATP synthase coupling factor 6 / ATP synthase delta/epsilon subunit, C-terminal domain superfamily / ATP synthase, F0 complex, subunit B/MI25 / ATP synthase, F0 complex, subunit B / Mitochondrial ATP synthase B chain precursor (ATP-synt_B) / ATP synthase, F0 complex, subunit D, mitochondrial / ATP synthase D chain, mitochondrial (ATP5H) / ATP synthase, F0 complex, subunit D superfamily, mitochondrial / ATP synthase, F0 complex, subunit A, bacterial/mitochondria / ATP synthase, F1 complex, epsilon subunit, mitochondrial / ATP synthase, F1 complex, epsilon subunit superfamily, mitochondrial / Mitochondrial ATP synthase epsilon chain / 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 / 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 peripheral stalk subunit OSCP / ATP synthase protein 8 / ATP synthase subunit a / ATP synthase subunit gamma, mitochondrial / ATP synthase F(0) complex subunit C1, mitochondrial / ATP synthase subunit alpha / ATP synthase membrane subunit DAPIT / ATP synthase subunit ATP5MPL, mitochondrial / ATP synthase subunit beta / ATP synthase subunit e, mitochondrial ...ATP synthase peripheral stalk subunit OSCP / ATP synthase protein 8 / ATP synthase subunit a / ATP synthase subunit gamma, mitochondrial / ATP synthase F(0) complex subunit C1, mitochondrial / ATP synthase subunit alpha / ATP synthase membrane subunit DAPIT / ATP synthase subunit ATP5MPL, mitochondrial / ATP synthase subunit beta / ATP synthase subunit e, mitochondrial / ATP synthase F1 subunit delta / ATP synthase subunit d, mitochondrial / ATP synthase peripheral stalk subunit OSCP / ATP synthase-coupling factor 6, mitochondrial / Uncharacterized protein / ATP synthase subunit / ATP synthase subunit f, mitochondrial / ATP synthase subunit b
Similarity search - Component
Biological speciesOvis aries (sheep) / Sheep (sheep)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsPinke G / Zhou L / Sazanov LA
CitationJournal: Nat Struct Mol Biol / Year: 2020
Title: Cryo-EM structure of the entire mammalian F-type ATP synthase.
Authors: Gergely Pinke / Long Zhou / Leonid A Sazanov /
Abstract: The majority of adenosine triphosphate (ATP) powering cellular processes in eukaryotes is produced by the mitochondrial F1Fo ATP synthase. Here, we present the atomic models of the membrane Fo domain ...The majority of adenosine triphosphate (ATP) powering cellular processes in eukaryotes is produced by the mitochondrial F1Fo ATP synthase. Here, we present the atomic models of the membrane Fo domain and the entire mammalian (ovine) F1Fo, determined by cryo-electron microscopy. Subunits in the membrane domain are arranged in the 'proton translocation cluster' attached to the c-ring and a more distant 'hook apparatus' holding subunit e. Unexpectedly, this subunit is anchored to a lipid 'plug' capping the c-ring. We present a detailed proton translocation pathway in mammalian Fo and key inter-monomer contacts in F1Fo multimers. Cryo-EM maps of F1Fo exposed to calcium reveal a retracted subunit e and a disassembled c-ring, suggesting permeability transition pore opening. We propose a model for the permeability transition pore opening, whereby subunit e pulls the lipid plug out of the c-ring. Our structure will allow the design of drugs for many emerging applications in medicine.
History
DepositionDec 23, 2019-
Header (metadata) releaseSep 23, 2020-
Map releaseSep 23, 2020-
UpdateDec 30, 2020-
Current statusDec 30, 2020Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.035
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 0.035
  • Imaged by UCSF Chimera
  • Download
  • Surface view with fitted model
  • Atomic models: PDB-6tt7
  • Surface level: 0.035
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

Downloads & links

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Map

FileDownload / File: emd_10573.map.gz / Format: CCP4 / Size: 16.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationComposite map of state 1a of ovine F1Fo, obtained from series of focused refinements as described in the paper.
Voxel sizeX=Y=Z: 1.061 Å
Density
Contour LevelBy AUTHOR: 0.035 / Movie #1: 0.035
Minimum - Maximum0.0 - 0.19801688
Average (Standard dev.)0.0052001504 (±0.015188017)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin000
Dimensions139230138
Spacing138139230
CellA: 146.418 Å / B: 147.479 Å / C: 244.03 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0611.0611.061
M x/y/z138139230
origin x/y/z0.0000.0000.000
length x/y/z146.418147.479244.030
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ138139230
MAP C/R/S321
start NC/NR/NS000
NC/NR/NS230139138
D min/max/mean0.0000.1980.005

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Supplemental data

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Mask #1

Fileemd_10573_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Supplemental map: emd 10573 additional 1.map

Fileemd_10573_additional_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Supplemental map: emd 10573 additional 2.map

Fileemd_10573_additional_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Supplemental map: emd 10573 additional 3.map

Fileemd_10573_additional_3.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Supplemental map: emd 10573 half map 1.map

Fileemd_10573_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Supplemental map: emd 10573 half map 2.map

Fileemd_10573_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : Purified ATP synthase from sheep heart mitochondria

EntireName: Purified ATP synthase from sheep heart mitochondria
Components
  • Complex: Purified ATP synthase from sheep heart mitochondria
    • Protein or peptide: ATP synthase subunit alpha
    • Protein or peptide: ATP synthase subunit beta
    • Protein or peptide: ATP synthase subunit gamma
    • Protein or peptide: ATP synthase F1 subunit delta
    • Protein or peptide: ATP synthase F1 subunit epsilon
    • Protein or peptide: ATP synthase peripheral stalk subunit OSCP
    • Protein or peptide: ATP synthase subunit b
    • Protein or peptide: ATP synthase-coupling factor 6, mitochondrial
    • Protein or peptide: ATP synthase subunit d, mitochondrial
    • Protein or peptide: ATP synthase F(0) complex subunit C1, mitochondrial
    • Protein or peptide: ATP synthase subunit a
    • Protein or peptide: Subunit DAPIT
    • Protein or peptide: ATP synthase membrane subunit 6.8PL
    • Protein or peptide: ATP synthase protein 8
    • Protein or peptide: ATP synthase membrane subunit f
    • Protein or peptide: ATP synthase subunit
    • Protein or peptide: Subunit e
  • Ligand: MAGNESIUM ION
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE
  • Ligand: O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine
  • Ligand: CARDIOLIPIN
  • Ligand: O-[(S)-hydroxy{[(2S)-2-hydroxy-3-(octadec-9-enoyloxy)propyl]oxy}phosphoryl]-L-serine

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Supramolecule #1: Purified ATP synthase from sheep heart mitochondria

SupramoleculeName: Purified ATP synthase from sheep heart mitochondria / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#17
Source (natural)Organism: Ovis aries (sheep)

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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
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 59.779492 KDa
SequenceString: MLSVRVAAAV ARALPRRAGL VSKNALGSSF IAARNLHASN SRLQKTGTAE VSSILEERIL GADTSVDLEE TGRVLSIGDG IARVHGLRN VQAEEMVEFS SGLKGMSLNL EPDNVGVVVF GNDKLIKEGD IVKRTGAIVD VPVGEELLGR VVDALGNAID G KGPIGSKA ...String:
MLSVRVAAAV ARALPRRAGL VSKNALGSSF IAARNLHASN SRLQKTGTAE VSSILEERIL GADTSVDLEE TGRVLSIGDG IARVHGLRN VQAEEMVEFS SGLKGMSLNL EPDNVGVVVF GNDKLIKEGD IVKRTGAIVD VPVGEELLGR VVDALGNAID G KGPIGSKA RRRVGLKAPG IIPRISVREP MQTGIKAVDS LVPIGRGQRE LIIGDRQTGK TSIAIDTIIN QKRFNDGTDE KK KLYCIYV AIGQKRSTVA QLVKRLTDAD AMKYTIVVSA TASDAAPLQY LAPYSGCSMG EYFRDNGKHA LIIYDDLSKQ AVA YRQMSL LLRRPPGREA YPGDVFYLHS RLLERAAKMN DAFGGGSLTA LPVIETQAGD VSAYIPTNVI SITDGQIFLE TELF YKGIR PAINVGLSVS RVGSAAQTRA MKQVAGTMKL ELAQYREVAA FAQFGSDLDA ATQQLLSRGV RLTELLKQGQ YSPMA IEEQ VAVIYAGVRG YLDKLEPSKI TKFENAFLSH VISQHQTLLG KIRTDGKISE EADAKLKEIV TNFLAGFEA

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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: Sheep (sheep)
Molecular weightTheoretical: 56.26509 KDa
SequenceString: MLGLVGRVAA ASASGALRGV NPSAPLPQAQ LLLRAAPAAL QPARDYAAQA SPSPKAGGAT GRIVAVIGAV VDVQFDEGLP PILNALEVQ GRETRLVLEV AQHLGESTVR TIAMDGTEGL VRGQKVLDSG APIRIPVGPE TLGRIMNVIG EPIDERGPIK T KQFAAIHA ...String:
MLGLVGRVAA ASASGALRGV NPSAPLPQAQ LLLRAAPAAL QPARDYAAQA SPSPKAGGAT GRIVAVIGAV VDVQFDEGLP PILNALEVQ GRETRLVLEV AQHLGESTVR TIAMDGTEGL VRGQKVLDSG APIRIPVGPE TLGRIMNVIG EPIDERGPIK T KQFAAIHA EAPEFVEMSV EQEILVTGIK VVDLLAPYAK GGKIGLFGGA GVGKTVLIME LINNVAKAHG GYSVFAGVGE RT REGNDLY HEMIESGVIN LKDATSKVAL VYGQMNEPPG ARARVALTGL TVAEYFRDQE GQDVLLFIDN IFRFTQAGSE VSA LLGRIP SAVGYQPTLA TDMGTMQERI TTTKKGSITS VQAIYVPADD LTDPAPATTF AHLDATTVLS RAIAELGIYP AVDP LDSTS RIMDPNIVGS EHYDVARGVQ KILQDYKSLQ DIIAILGMDE LSEEDKLTVS RARKIQRFLS QPFQVAEVFT GHLGK LVPL KETIKGFQQI LAGEFDHLPE QAFYMVGPIE EAVAKADKLA EEHS

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Macromolecule #3: ATP synthase subunit gamma

MacromoleculeName: ATP synthase subunit gamma / type: protein_or_peptide / ID: 3 / Details: XP_004014229.1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 33.133062 KDa
SequenceString: MFSRAGVAGL SAWTVQPQWI QVRNMATLKD ITRRLKSIKN IQKITKSMKM VAAAKYARAE RELKPARVYG VGSLALYEKA DIKTPEDKK KHLIIGVSSD RGLCGAIHSS VAKQMKSEAA NLAAAGKEVK IIGVGDKIRS ILHRTHSDQF LVTFKEVGRR P PTFGDASV ...String:
MFSRAGVAGL SAWTVQPQWI QVRNMATLKD ITRRLKSIKN IQKITKSMKM VAAAKYARAE RELKPARVYG VGSLALYEKA DIKTPEDKK KHLIIGVSSD RGLCGAIHSS VAKQMKSEAA NLAAAGKEVK IIGVGDKIRS ILHRTHSDQF LVTFKEVGRR P PTFGDASV IALELLNSGY EFDEGSIIFN RFRSVISYKT EEKPIFSLDT ISSAESMSIY DDIDADVLRN YQEYSLANII YY SLKESTT SEQSARMTAM DNASKNASEM IDKLTLTFNR TRQAVITKEL IEIISGAAAL E

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Macromolecule #4: ATP synthase F1 subunit delta

MacromoleculeName: ATP synthase F1 subunit delta / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 17.580924 KDa
SequenceString:
MLPSALLRRP GLGRLVRQVR AYAEAAPAQA PAAGPGQMSF TFASPTQVFF NGANVRQVDV PTQTGAFGIL AAHVPTLQVL RPGLVVVHA EDGTTSKYFV SSGSVTVNAD SSVQLLAEEA VTLDMLDLGA AKANLEKAQS ELLGAADEAT RAEIQIRIEA N EALVKALE

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Macromolecule #5: ATP synthase F1 subunit epsilon

MacromoleculeName: ATP synthase F1 subunit epsilon / type: protein_or_peptide / ID: 5 / Details: XP_027832792.1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 5.779863 KDa
SequenceString:
MVAYWRQAGL SYIRYSQICA KAVRDALKTE FKANAMKTSG SSIKIVKVKK E

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Macromolecule #6: ATP synthase peripheral stalk subunit OSCP

MacromoleculeName: ATP synthase peripheral stalk subunit OSCP / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 23.435695 KDa
SequenceString: MAALAVSGLS QQVRCFSTSV VRPFAKLVRP PVQIYGIEGR YATALYSAAS KQNKLEQVEK ELLRVGQILK EPKMAASLMN PYVKRSVKV KSLNDMTAKE KFSPLTSNLI NLLAENGRLN NTPAVISAFS TMMSVHRGEV PCTVTTASPL DEATLTELKT V LKSFLSKG ...String:
MAALAVSGLS QQVRCFSTSV VRPFAKLVRP PVQIYGIEGR YATALYSAAS KQNKLEQVEK ELLRVGQILK EPKMAASLMN PYVKRSVKV KSLNDMTAKE KFSPLTSNLI NLLAENGRLN NTPAVISAFS TMMSVHRGEV PCTVTTASPL DEATLTELKT V LKSFLSKG QVLKLEVKID PSIMGGMIVR IGEKYVDMSA KTKIQKLSRA MREIL

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Macromolecule #7: ATP synthase subunit b

MacromoleculeName: ATP synthase subunit b / type: protein_or_peptide / ID: 7 / Details: XP_004002367.2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 28.84457 KDa
SequenceString: MLSRVVLSAA AAAAPSLKNA AFLGPGVLQA TRIFHTGQPS LAPVPPLPEH GGKVRFGLIP EEFFQFLYPK TGVTGPYVLG TGLILYLLS KEIYVITPET FSAISTIGFL VYVVKKYGAS VGEFADKLNE QKIAQLEEVK QASIKQIQDA IDMEKSQQAL V QKRHYLFD ...String:
MLSRVVLSAA AAAAPSLKNA AFLGPGVLQA TRIFHTGQPS LAPVPPLPEH GGKVRFGLIP EEFFQFLYPK TGVTGPYVLG TGLILYLLS KEIYVITPET FSAISTIGFL VYVVKKYGAS VGEFADKLNE QKIAQLEEVK QASIKQIQDA IDMEKSQQAL V QKRHYLFD VQRNNIAMAL EVTYRERLHR VYREVKNRLD YHISVQNMMR QKEQEHMINW VEKHVVQSIS AQQEKETIAK CI ADLKLLA KKAQAQPVM

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Macromolecule #8: ATP synthase-coupling factor 6, mitochondrial

MacromoleculeName: ATP synthase-coupling factor 6, mitochondrial / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 12.490296 KDa
SequenceString:
MILQRLFRLS SVVQSAISVS LRRNIGVTAV AFNKELDPVQ KLFVDKIREY RTKRQTSGGP VDAGPEYQQD LDRELFKLKQ MYGKADMNT FPNFTFEDPK FEVVEKPQS

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Macromolecule #9: ATP synthase subunit d, mitochondrial

MacromoleculeName: ATP synthase subunit d, mitochondrial / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 18.747508 KDa
SequenceString:
MAGRKLALKT IDWVAFGEII PRNQKAVANS LKSWNETLTS RLATLPEKPP AIDWAYYKAN VTKAGLVDDF EKKFNALKVP IPEDKYTAQ VDAEEKEDVK SCAEFLIQSK TRIQEYEKEL EKMRNIIPFD QMTIEDLNEV FPETKLDKKK YPYWPHRPIE S L

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Macromolecule #10: ATP synthase F(0) complex subunit C1, mitochondrial

MacromoleculeName: ATP synthase F(0) complex subunit C1, mitochondrial / type: protein_or_peptide / ID: 10 / Number of copies: 8 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 14.201577 KDa
SequenceString:
MQTTGALLIS PALIRSCTRG LIRPVSASFL SRPEIPSVQP SYSSGPLQVA RREFQTSVVS RDIDTAAKFI GAGAATVGVA GSGAGIGTV FGSLIIGYAR NPSLKQQLFS YAILGFALSE AMGLFCLMVA FLILFAM

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Macromolecule #11: ATP synthase subunit a

MacromoleculeName: ATP synthase subunit a / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 24.81185 KDa
SequenceString: MNENLFASFI TPMMFGLPLV TLIVLFPSLL FPTSNRLVNN RLISLQQWML QLVSKQMMSI HNTKGQTWAL MLMSLILFIG STNLLGLLP HSFTPTTQLS MNLGMAIPLW GGAVITGFRN KTKASLAHFL PQGTPTPLIP MLVIIETISL FIQPVALAVR L TANITAGH ...String:
MNENLFASFI TPMMFGLPLV TLIVLFPSLL FPTSNRLVNN RLISLQQWML QLVSKQMMSI HNTKGQTWAL MLMSLILFIG STNLLGLLP HSFTPTTQLS MNLGMAIPLW GGAVITGFRN KTKASLAHFL PQGTPTPLIP MLVIIETISL FIQPVALAVR L TANITAGH LLIHLIGGAT LALMSINTTT ALITFIILIL LTVLEFAVAM IQAYVFTLLV SLYLHDNT

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Macromolecule #12: Subunit DAPIT

MacromoleculeName: Subunit DAPIT / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 6.443579 KDa
SequenceString:
MAGPEADAQF HFTGIKKYFN SYTLTGRMNC VLATYGSIAL IVLYFKLRSK KTPAVKAT

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Macromolecule #13: ATP synthase membrane subunit 6.8PL

MacromoleculeName: ATP synthase membrane subunit 6.8PL / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 6.846093 KDa
SequenceString:
MLQSLIKKVW IPMKPYYTQA YQEIWVGTGL MAYIVYKIRS ADKRSKALKA SSAAPAHGHH

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Macromolecule #14: ATP synthase protein 8

MacromoleculeName: ATP synthase protein 8 / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 7.918443 KDa
SequenceString:
MPQLDTSTWL TMILSMFLVL FIIFQLKISK HNFYHNPELM TTKTPKQNTP WETKWTKIYL PLSLPL

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Macromolecule #15: ATP synthase membrane subunit f

MacromoleculeName: ATP synthase membrane subunit f / type: protein_or_peptide / ID: 15 / Details: XP_004016938.3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 10.315207 KDa
SequenceString:
MASVVPLKEK KLLEVKLGEL PSWILMRDFT PSGIAGAFQR GYYRYYNKYV NVKKGSIAGL SMVLAAYVFL NYCRSYKELK HERLRKYH

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Macromolecule #16: ATP synthase subunit

MacromoleculeName: ATP synthase subunit / type: protein_or_peptide / ID: 16 / Details: XP_011950914.1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 11.428407 KDa
SequenceString:
MAQFVRNLAE KAPALVNAAV TYSKPRLATF WYYAKVELVP PTPAEIPTAI QSLKKIINSA KTGSFKQLTV KEALLNGLVA TEVWMWFYV GEIIGKRGII GYDV

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Macromolecule #17: Subunit e

MacromoleculeName: Subunit e / type: protein_or_peptide / ID: 17 / Details: XP_027827162.1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep)
Molecular weightTheoretical: 8.336688 KDa
SequenceString:
MVPPVQVSPL IKLGRYSALF LGMAYGAKRY NYLKPRAEEE RRLAAEEKKK RDEQKRIERE LAEAQEDTIL K

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Macromolecule #18: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 18 / Number of copies: 3 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #19: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 19 / Number of copies: 5 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

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

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Macromolecule #20: 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE

MacromoleculeName: 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE / type: ligand / ID: 20 / Number of copies: 6 / Formula: LHG
Molecular weightTheoretical: 722.97 Da
Chemical component information

ChemComp-LHG:
1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE / phospholipid*YM / Phosphatidylglycerol

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Macromolecule #21: O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phospho...

MacromoleculeName: O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine
type: ligand / ID: 21 / Number of copies: 1 / Formula: P5S
Molecular weightTheoretical: 792.075 Da
Chemical component information

ChemComp-P5S:
O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine / Phosphatidylserine

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Macromolecule #22: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 22 / Number of copies: 3 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM / Cardiolipin

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Macromolecule #23: O-[(S)-hydroxy{[(2S)-2-hydroxy-3-(octadec-9-enoyloxy)propyl]oxy}p...

MacromoleculeName: O-[(S)-hydroxy{[(2S)-2-hydroxy-3-(octadec-9-enoyloxy)propyl]oxy}phosphoryl]-L-serine
type: ligand / ID: 23 / Number of copies: 1 / Formula: S12
Molecular weightTheoretical: 523.597 Da
Chemical component information

ChemComp-S12:
O-[(S)-hydroxy{[(2S)-2-hydroxy-3-(octadec-9-enoyloxy)propyl]oxy}phosphoryl]-L-serine

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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

Concentration2.8 mg/mL
BufferpH: 7.4
Details: 20 mM HEPES pH7.4, 35 mM NaCl, 2 mM EDTA, 1% sucrose, 1 mM DTT, 0.1% LMNG, 0.2% CHAPS
GridModel: Quantifoil R0.6/1 / Material: COPPER / Mesh: 400 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: AIR
VitrificationCryogen name: ETHANE-PROPANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsCalibrated defocus max: 2.4 µm / Calibrated defocus min: 1.0 µm / Calibrated magnification: 131951 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Detector mode: INTEGRATING / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Digitization - Sampling interval: 14.0 µm / Number grids imaged: 1 / Number real images: 3053 / Average exposure time: 1.0 sec. / Average electron dose: 106.0 e/Å2 / Details: 40 frames per movie
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 809000
CTF correctionSoftware - Name: CTFFIND (ver. 4.1.13)
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0)
Final 3D classificationSoftware - Name: RELION (ver. 3.0)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0)
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0) / Number images used: 35000
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:
RefinementSpace: REAL / Protocol: AB INITIO MODEL
Output model

PDB-6tt7:
Ovine ATP synthase 1a state

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Atomic model buiding 2

Initial modelPDB ID:
RefinementSpace: REAL / Protocol: AB INITIO MODEL / Overall B value: 96
Output model

PDB-6tt7:
Ovine ATP synthase 1a state

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