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- EMDB-65577: Cryo-EM structure of FoF1-ATPase monomer state 1 on the bovine he... -

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Basic information

Entry
Database: EMDB / ID: EMD-65577
TitleCryo-EM structure of FoF1-ATPase monomer state 1 on the bovine heart submitochondrial particles (FoF1-1)
Map data
Sample
  • Complex: FoF1-ATPase on the bovine heart submitochondrial particles
    • Protein or peptide: x 18 types
  • Ligand: x 3 types
KeywordsATP synthase / FoF1-ATPase / submitochondrial particles / MOTOR PROTEIN
Function / homology
Function and homology information


Mitochondrial protein import / negative regulation of mitochondrial ATP synthesis coupled proton transport / angiostatin binding / negative regulation of hydrolase activity / Formation of ATP by chemiosmotic coupling / Cristae formation / ATPase inhibitor activity / mitochondrial proton-transporting ATP synthase complex assembly / mitochondrial envelope / Mitochondrial translation termination ...Mitochondrial protein import / negative regulation of mitochondrial ATP synthesis coupled proton transport / angiostatin binding / negative regulation of hydrolase activity / Formation of ATP by chemiosmotic coupling / Cristae formation / ATPase inhibitor activity / mitochondrial proton-transporting ATP synthase complex assembly / mitochondrial envelope / Mitochondrial translation termination / proton channel activity / heme biosynthetic process / Mitochondrial protein degradation / negative regulation of endothelial cell proliferation / proton transmembrane transporter activity / proton motive force-driven ATP synthesis / proton-transporting two-sector ATPase complex, proton-transporting domain / proton motive force-driven mitochondrial ATP synthesis / H+-transporting two-sector ATPase / proton-transporting ATP synthase complex / proton-transporting ATP synthase activity, rotational mechanism / proton transmembrane transport / aerobic respiration / erythrocyte differentiation / ADP binding / mitochondrial membrane / ATPase binding / protein homotetramerization / calmodulin binding / mitochondrial inner membrane / lipid binding / structural molecule activity / cell surface / protein homodimerization activity / ATP hydrolysis activity / protein-containing complex / mitochondrion / ATP binding / metal ion binding / identical protein binding / plasma membrane / cytoplasm
Similarity search - Function
ATP synthase membrane subunit K / ATP synthase regulation / ATP synthase subunit ATP5MJ, mitochondrial / Mitochondrial proteolipid / ATP synthase, F0 complex, subunit G, mitochondrial / ATP synthase, F0 complex, subunit E, mitochondrial / Mitochondrial ATP synthase subunit g, animal / Mitochondrial ATP synthase g subunit / ATP synthase E chain / ATP synthase protein 8, metazoa ...ATP synthase membrane subunit K / ATP synthase regulation / ATP synthase subunit ATP5MJ, mitochondrial / Mitochondrial proteolipid / ATP synthase, F0 complex, subunit G, mitochondrial / ATP synthase, F0 complex, subunit E, mitochondrial / Mitochondrial ATP synthase subunit g, animal / Mitochondrial ATP synthase g subunit / ATP synthase E chain / ATP synthase protein 8, metazoa / Mitochondrial ATPase inhibitor / Mitochondrial F1-F0 ATP synthase subunit F, predicted / ATP synthase protein 8, mammals / ATP synthase protein 8 / Mitochondrial ATPase inhibitor, IATP / 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 / : / Metazoan delta subunit of F1F0-ATP synthase, C-terminal domain / 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 delta/epsilon subunit, C-terminal domain superfamily / 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, 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 F(1) complex catalytic subunit beta, mitochondrial / ATP synthase F(0) complex subunit a / ATPase inhibitor, mitochondrial / ATP synthase peripheral stalk subunit F6, mitochondrial / ATP synthase F(0) complex subunit 8 / ATP synthase F(1) complex subunit delta, mitochondrial / ATP synthase F(1) complex subunit gamma, mitochondrial / ATP synthase F(1) complex subunit epsilon, mitochondrial / ATP synthase peripheral stalk subunit b, mitochondrial / ATP synthase peripheral stalk subunit d, mitochondrial ...ATP synthase F(1) complex catalytic subunit beta, mitochondrial / ATP synthase F(0) complex subunit a / ATPase inhibitor, mitochondrial / ATP synthase peripheral stalk subunit F6, mitochondrial / ATP synthase F(0) complex subunit 8 / ATP synthase F(1) complex subunit delta, mitochondrial / ATP synthase F(1) complex subunit gamma, mitochondrial / ATP synthase F(1) complex subunit epsilon, mitochondrial / ATP synthase peripheral stalk subunit b, mitochondrial / ATP synthase peripheral stalk subunit d, mitochondrial / ATP synthase peripheral stalk subunit OSCP, mitochondrial / ATP synthase F(0) complex subunit j, mitochondrial / ATP synthase F(1) complex subunit alpha, mitochondrial / ATP synthase F(0) complex subunit C1, mitochondrial / ATP synthase F(0) complex subunit e, mitochondrial / ATP synthase F(0) complex subunit f, mitochondrial / ATP synthase F(0) complex subunit g, mitochondrial / ATP synthase F(0) complex subunit k, mitochondrial
Similarity search - Component
Biological speciesBos taurus (domestic cattle)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsNakano A / Masuya T / Akisada S / Ishikawa-Fukuda M / Mitsuoka K / Miyoshi H / Murai M / Yokoyama K
Funding support Japan, 3 items
OrganizationGrant numberCountry
Japan Society for the Promotion of Science (JSPS)23H02453 Japan
Japan Society for the Promotion of Science (JSPS)25K01958 Japan
Ministry of Education, Culture, Sports, Science and Technology (Japan) Japan
CitationJournal: Nat Commun / Year: 2026
Title: Structures of respiratory supercomplexes and ATP synthase oligomers in mammalian mitochondrial inner membrane.
Authors: Atsuki Nakano / Takahiro Masuya / Shinsuke Akisada / Moe Ishikawa-Fukuda / Kaoru Mitsuoka / Hideto Miyoshi / Masatoshi Murai / Ken Yokoyama /
Abstract: Understanding the functional mechanisms of membrane protein complexes requires structural analysis within their native membrane environment. Here, we applied cryo-electron microscopy to determine the ...Understanding the functional mechanisms of membrane protein complexes requires structural analysis within their native membrane environment. Here, we applied cryo-electron microscopy to determine the structures of FF ATP synthase and respiratory supercomplexes (SCs) on sub-mitochondrial particles (SMPs) isolated from bovine heart mitochondria. Most FF complexes were observed as dimers stabilized by the regulatory factor IF₁, and a tetrameric assembly comprising two FF-IF₁ dimers arranged linearly was also identified. This finding indicates that the tetrameric units of FF are present in the mitochondrial inner membrane and contribute to shaping cristae tips in mammalian mitochondria. F domain maps resolve the e-subunit- c₈-ring interface and show no discrete density for a tightly bound lipid within the c₈-ring. In addition to the previously reported SCs compositions CI₁CIII₂CIV₁ and CI₁CIII₂CIV₂, our analysis identified an additional assembly with the composition CI₁CIII₂CIV₃, as well as a CI₂CIII₂CIV₆ mega-complex. This approach enables rapid structural determination of FF ATP synthase and SCs from minimal membrane fractions, providing a foundation for elucidating the molecular basis of metabolic disorders and mitochondrial diseases at the level of higher-order architecture.
History
DepositionJul 28, 2025-
Header (metadata) releaseApr 1, 2026-
Map releaseApr 1, 2026-
UpdateApr 1, 2026-
Current statusApr 1, 2026Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_65577.png

Downloads & links

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Map

FileDownload / File: emd_65577.map.gz / Format: CCP4 / Size: 347.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

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AxesZ (Sec.)Y (Row.)X (Col.)
1.45 Å/pix.
x 450 pix.
= 654. Å		1.45 Å/pix.
x 450 pix.
= 654. Å		1.45 Å/pix.
x 450 pix.
= 654. Å

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.45333 Å
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Histogram (log scale)
Contour LevelBy AUTHOR: 0.2
Minimum - Maximum-1.3819592 - 1.9557265
Average (Standard dev.)-0.000059841626 (±0.03258302)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions450450450
Spacing450450450
CellA=B=C: 654.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_65577_msk_1.map
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Half map: #2

Fileemd_65577_half_map_1.map
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Half map: #1

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Sample components

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Entire : FoF1-ATPase on the bovine heart submitochondrial particles

EntireName: FoF1-ATPase on the bovine heart submitochondrial particles
Components
  • Complex: FoF1-ATPase on the bovine heart submitochondrial particles
    • Protein or peptide: ATP synthase F(0) complex subunit 8
    • Protein or peptide: ATP synthase F(1) complex subunit alpha, mitochondrial
    • Protein or peptide: ATP synthase F(1) complex catalytic subunit beta, mitochondrial
    • Protein or peptide: ATP synthase F(1) complex subunit gamma, mitochondrial
    • Protein or peptide: ATP synthase F(1) complex subunit delta, mitochondrial
    • Protein or peptide: ATP synthase F(1) complex subunit epsilon, mitochondrial
    • Protein or peptide: ATPase inhibitor, mitochondrial
    • Protein or peptide: ATP synthase F(0) complex subunit C1, mitochondrial
    • Protein or peptide: ATP synthase peripheral stalk subunit OSCP, mitochondrial
    • Protein or peptide: ATP synthase F(0) complex subunit a
    • Protein or peptide: ATP synthase peripheral stalk subunit b, mitochondrial
    • Protein or peptide: ATP synthase peripheral stalk subunit d, mitochondrial
    • Protein or peptide: ATP synthase F(0) complex subunit e, mitochondrial
    • Protein or peptide: ATP synthase F(0) complex subunit f, mitochondrial
    • Protein or peptide: ATP synthase F(0) complex subunit g, mitochondrial
    • Protein or peptide: ATP synthase peripheral stalk subunit F6, mitochondrial
    • Protein or peptide: ATP synthase F(0) complex subunit j, mitochondrial
    • Protein or peptide: ATP synthase F(0) complex subunit k, mitochondrial
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: ADENOSINE-5'-DIPHOSPHATE

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Supramolecule #1: FoF1-ATPase on the bovine heart submitochondrial particles

SupramoleculeName: FoF1-ATPase on the bovine heart submitochondrial particles
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#18
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 600 KDa

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Macromolecule #1: ATP synthase F(0) complex subunit 8

MacromoleculeName: ATP synthase F(0) complex subunit 8 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 7.944523 KDa
SequenceString:
MPQLDTSTWL TMILSMFLTL FIIFQLKVSK HNFYHNPELT PTKMLKQNTP WETKWTKIYL PLLLPL

UniProtKB: ATP synthase F(0) complex subunit 8

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Macromolecule #2: ATP synthase F(1) complex subunit alpha, mitochondrial

MacromoleculeName: ATP synthase F(1) complex subunit alpha, mitochondrial
type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 55.331234 KDa
SequenceString: QKTGTAEVSS ILEERILGAD TSVDLEETGR VLSIGDGIAR VHGLRNVQAE EMVEFSSGLK GMSLNLEPDN VGVVVFGNDK LIKEGDIVK RTGAIVDVPV GEELLGRVVD ALGNAIDGKG PIGSKARRRV GLKAPGIIPR ISVREPMQTG IKAVDSLVPI G RGQRELII ...String:
QKTGTAEVSS ILEERILGAD TSVDLEETGR VLSIGDGIAR VHGLRNVQAE EMVEFSSGLK GMSLNLEPDN VGVVVFGNDK LIKEGDIVK RTGAIVDVPV GEELLGRVVD ALGNAIDGKG PIGSKARRRV GLKAPGIIPR ISVREPMQTG IKAVDSLVPI G RGQRELII GDRQTGKTSI AIDTIINQKR FNDGTDEKKK LYCIYVAIGQ KRSTVAQLVK RLTDADAMKY TIVVSATASD AA PLQYLAP YSGCSMGEYF RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE RAAKMNDAFG GGS LTALPV IETQAGDVSA YIPTNVISIT DGQIFLETEL FYKGIRPAIN VGLSVSRVGS AAQTRAMKQV AGTMKLELAQ YREV AAFAQ FGSDLDAATQ QLLSRGVRLT ELLKQGQYSP MAIEEQVAVI YAGVRGYLDK LEPSKITKFE NAFLSHVISQ HQALL SKIR TDGKISEESD AKLKEIVTNF LAGFEA

UniProtKB: ATP synthase F(1) complex subunit alpha, mitochondrial

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Macromolecule #3: ATP synthase F(1) complex catalytic subunit beta, mitochondrial

MacromoleculeName: ATP synthase F(1) complex catalytic subunit beta, mitochondrial
type: protein_or_peptide / ID: 3 / Number of copies: 3 / Enantiomer: LEVO / EC number: H+-transporting two-sector ATPase
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 51.757836 KDa
SequenceString: AAQASPSPKA GATTGRIVAV IGAVVDVQFD EGLPPILNAL EVQGRETRLV LEVAQHLGES TVRTIAMDGT EGLVRGQKVL DSGAPIRIP VGPETLGRIM NVIGEPIDER GPIKTKQFAA IHAEAPEFVE MSVEQEILVT GIKVVDLLAP YAKGGKIGLF G GAGVGKTV ...String:
AAQASPSPKA GATTGRIVAV IGAVVDVQFD EGLPPILNAL EVQGRETRLV LEVAQHLGES TVRTIAMDGT EGLVRGQKVL DSGAPIRIP VGPETLGRIM NVIGEPIDER GPIKTKQFAA IHAEAPEFVE MSVEQEILVT GIKVVDLLAP YAKGGKIGLF G GAGVGKTV LIMELINNVA KAHGGYSVFA GVGERTREGN DLYHEMIESG VINLKDATSK VALVYGQMNE PPGARARVAL TG LTVAEYF RDQEGQDVLL FIDNIFRFTQ AGSEVSALLG RIPSAVGYQP TLATDMGTMQ ERITTTKKGS ITSVQAIYVP ADD LTDPAP ATTFAHLDAT TVLSRAIAEL GIYPAVDPLD STSRIMDPNI VGSEHYDVAR GVQKILQDYK SLQDIIAILG MDEL SEEDK LTVSRARKIQ RFLSQPFQVA EVFTGHLGKL VPLKETIKGF QQILAGEYDH LPEQAFYMVG PIEEAVAKAD KLAEE HS

UniProtKB: ATP synthase F(1) complex catalytic subunit beta, mitochondrial

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Macromolecule #4: ATP synthase F(1) complex subunit gamma, mitochondrial

MacromoleculeName: ATP synthase F(1) complex subunit gamma, mitochondrial
type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 30.30076 KDa
SequenceString: ATLKDITRRL KSIKNIQKIT KSMKMVAAAK YARAERELKP ARVYGVGSLA LYEKADIKTP EDKKKHLIIG VSSDRGLCGA IHSSVAKQM KSEAANLAAA GKEVKIIGVG DKIRSILHRT HSDQFLVTFK EVGRRPPTFG DASVIALELL NSGYEFDEGS I IFNRFRSV ...String:
ATLKDITRRL KSIKNIQKIT KSMKMVAAAK YARAERELKP ARVYGVGSLA LYEKADIKTP EDKKKHLIIG VSSDRGLCGA IHSSVAKQM KSEAANLAAA GKEVKIIGVG DKIRSILHRT HSDQFLVTFK EVGRRPPTFG DASVIALELL NSGYEFDEGS I IFNRFRSV ISYKTEEKPI FSLDTISSAE SMSIYDDIDA DVLRNYQEYS LANIIYYSLK ESTTSEQSAR MTAMDNASKN AS EMIDKLT LTFNRTRQAV ITKELIEIIS GAAALD

UniProtKB: ATP synthase F(1) complex subunit gamma, mitochondrial

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Macromolecule #5: ATP synthase F(1) complex subunit delta, mitochondrial

MacromoleculeName: ATP synthase F(1) complex subunit delta, mitochondrial
type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 15.074813 KDa
SequenceString:
AEAAAAQAPA AGPGQMSFTF ASPTQVFFNS ANVRQVDVPT QTGAFGILAA HVPTLQVLRP GLVVVHAEDG TTSKYFVSSG SVTVNADSS VQLLAEEAVT LDMLDLGAAK ANLEKAQSEL LGAADEATRA EIQIRIEANE ALVKALE

UniProtKB: ATP synthase F(1) complex subunit delta, mitochondrial

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Macromolecule #6: ATP synthase F(1) complex subunit epsilon, mitochondrial

MacromoleculeName: ATP synthase F(1) complex subunit epsilon, mitochondrial
type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 5.662693 KDa
SequenceString:
VAYWRQAGLS YIRYSQICAK AVRDALKTEF KANAMKTSGS TIKIVKVKKE

UniProtKB: ATP synthase F(1) complex subunit epsilon, mitochondrial

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Macromolecule #7: ATPase inhibitor, mitochondrial

MacromoleculeName: ATPase inhibitor, mitochondrial / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 6.633216 KDa
SequenceString:
GSESGDNVRS SAGAVRDAGG AFGKREQAEE ERYFRARAKE QLAALKKHHE NEISHHAKEI

UniProtKB: ATPase inhibitor, mitochondrial

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Macromolecule #8: ATP synthase F(0) complex subunit C1, mitochondrial

MacromoleculeName: ATP synthase F(0) complex subunit C1, mitochondrial / type: protein_or_peptide / ID: 8 / Number of copies: 8 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 7.653034 KDa
SequenceString:
DIDTAAKFIG AGAATVGVAG SGAGIGTVFG SLIIGYARNP SL(M3L)QQLFSYA ILGFALSEAM GLFCLMVAFL ILFAM

UniProtKB: ATP synthase F(0) complex subunit C1, mitochondrial

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Macromolecule #9: ATP synthase peripheral stalk subunit OSCP, mitochondrial

MacromoleculeName: ATP synthase peripheral stalk subunit OSCP, mitochondrial
type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 20.959777 KDa
SequenceString:
FAKLVRPPVQ IYGIEGRYAT ALYSAASKQN KLEQVEKELL RVGQILKEPK MAASLLNPYV KRSVKVKSLS DMTAKEKFSP LTSNLINLL AENGRLTNTP AVISAFSTMM SVHRGEVPCT VTTASALDEA TLTELKTVLK SFLSKGQVLK LEVKIDPSIM G GMIVRIGE KYVDMSAKTK IQKLSRAMRE IL

UniProtKB: ATP synthase peripheral stalk subunit OSCP, mitochondrial

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Macromolecule #10: ATP synthase F(0) complex subunit a

MacromoleculeName: ATP synthase F(0) complex subunit a / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 24.801785 KDa
SequenceString: MNENLFTSFI TPVILGLPLV TLIVLFPSLL FPTSNRLVSN RFVTLQQWML QLVSKQMMSI HNSKGQTWTL MLMSLILFIG STNLLGLLP HSFTPTTQLS MNLGMAIPLW AGAVITGFRN KTKASLAHFL PQGTPTPLIP MLVIIETISL FIQPMALAVR L TANITAGH ...String:
MNENLFTSFI TPVILGLPLV TLIVLFPSLL FPTSNRLVSN RFVTLQQWML QLVSKQMMSI HNSKGQTWTL MLMSLILFIG STNLLGLLP HSFTPTTQLS MNLGMAIPLW AGAVITGFRN KTKASLAHFL PQGTPTPLIP MLVIIETISL FIQPMALAVR L TANITAGH LLIHLIGGAT LALMSISTTT ALITFTILIL LTILEFAVAM IQAYVFTLLV SLYLHDNT

UniProtKB: ATP synthase F(0) complex subunit a

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Macromolecule #11: ATP synthase peripheral stalk subunit b, mitochondrial

MacromoleculeName: ATP synthase peripheral stalk subunit b, mitochondrial
type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 24.702709 KDa
SequenceString: PVPPLPEHGG KVRFGLIPEE FFQFLYPKTG VTGPYVLGTG LILYLLSKEI YVITPETFSA ISTIGFLVYI VKKYGASVGE FADKLNEQK IAQLEEVKQA SIKQIQDAID MEKSQQALVQ KRHYLFDVQR NNIAMALEVT YRERLHRVYR EVKNRLDYHI S VQNMMRQK ...String:
PVPPLPEHGG KVRFGLIPEE FFQFLYPKTG VTGPYVLGTG LILYLLSKEI YVITPETFSA ISTIGFLVYI VKKYGASVGE FADKLNEQK IAQLEEVKQA SIKQIQDAID MEKSQQALVQ KRHYLFDVQR NNIAMALEVT YRERLHRVYR EVKNRLDYHI S VQNMMRQK EQEHMINWVE KRVVQSISAQ QEKETIAKCI ADLKLLSKKA QAQPVM

UniProtKB: ATP synthase peripheral stalk subunit b, mitochondrial

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Macromolecule #12: ATP synthase peripheral stalk subunit d, mitochondrial

MacromoleculeName: ATP synthase peripheral stalk subunit d, mitochondrial
type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 18.588256 KDa
SequenceString:
AGRKLALKTI DWVAFGEIIP RNQKAVANSL KSWNETLTSR LATLPEKPPA IDWAYYKANV AKAGLVDDFE KKFNALKVPI PEDKYTAQV DAEEKEDVKS CAEFLTQSKT RIQEYEKELE KMRNIIPFDQ MTIEDLNEVF PETKLDKKKY PYWPHRPIET L

UniProtKB: ATP synthase peripheral stalk subunit d, mitochondrial

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Macromolecule #13: ATP synthase F(0) complex subunit e, mitochondrial

MacromoleculeName: ATP synthase F(0) complex subunit e, mitochondrial / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 8.205492 KDa
SequenceString:
VPPVQVSPLI KLGRYSALFL GMAYGAKRYN YLKPRAEEER RLAAEEKKKR DEQKRIEREL AEAQEDTILK

UniProtKB: ATP synthase F(0) complex subunit e, mitochondrial

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Macromolecule #14: ATP synthase F(0) complex subunit f, mitochondrial

MacromoleculeName: ATP synthase F(0) complex subunit f, mitochondrial / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 10.184011 KDa
SequenceString:
ASVVPLKEKK LLEVKLGELP SWILMRDFTP SGIAGAFQRG YYRYYNKYVN VKKGSIAGLS MVLAAYVFLN YCRSYKELKH ERLRKYH

UniProtKB: ATP synthase F(0) complex subunit f, mitochondrial

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Macromolecule #15: ATP synthase F(0) complex subunit g, mitochondrial

MacromoleculeName: ATP synthase F(0) complex subunit g, mitochondrial / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 11.298196 KDa
SequenceString:
AEFVRNLAEK APALVNAAVT YSKPRLATFW YYAKVELVPP TPAEIPTAIQ SLKKIINSAK TGSFKQLTVK EALLNGLVAT EVWMWFYVG EIIGKRGIIG YDV

UniProtKB: ATP synthase F(0) complex subunit g, mitochondrial

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Macromolecule #16: ATP synthase peripheral stalk subunit F6, mitochondrial

MacromoleculeName: ATP synthase peripheral stalk subunit F6, mitochondrial
type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 8.971079 KDa
SequenceString:
NKELDPVQKL FVDKIREYRT KRQTSGGPVD AGPEYQQDLD RELFKLKQMY GKADMNTFPN FTFEDPKFEV VEKPQS

UniProtKB: ATP synthase peripheral stalk subunit F6, mitochondrial

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Macromolecule #17: ATP synthase F(0) complex subunit j, mitochondrial

MacromoleculeName: ATP synthase F(0) complex subunit j, mitochondrial / type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 6.846093 KDa
SequenceString:
MLQSLIKKVW IPMKPYYTQA YQEIWVGTGL MAYIVYKIRS ADKRSKALKA SSAAPAHGHH

UniProtKB: ATP synthase F(0) complex subunit j, mitochondrial

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Macromolecule #18: ATP synthase F(0) complex subunit k, mitochondrial

MacromoleculeName: ATP synthase F(0) complex subunit k, mitochondrial / type: protein_or_peptide / ID: 18 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 6.312383 KDa
SequenceString:
AGPEADAQFH FTGIKKYFNS YTLTGRMNCV LATYGSIALI VLYFKLRSKK TPAVKAT

UniProtKB: ATP synthase F(0) complex subunit k, mitochondrial

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Macromolecule #19: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 19 / 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 #20: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 20 / Number of copies: 5 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #21: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 21 / Number of copies: 1 / 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 / Chamber humidity: 100 % / Chamber temperature: 298 K

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (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: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.8 µm / Nominal defocus min: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 30421492
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionAlgorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.7) / Number images used: 328822
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

6zpo


Chain - Source name: PDB / Chain - Initial model type: experimental model
RefinementSpace: REAL / Protocol: FLEXIBLE FIT
Output model

PDB-9w2r:
Cryo-EM structure of FoF1-ATPase monomer state 1 on the bovine heart submitochondrial particles (FoF1-1)

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