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- EMDB-10861: Cryo-EM structure of Tetrahymena thermophila mitochondrial ATP sy... -

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Basic information

Entry
Database: EMDB / ID: EMD-10861
TitleCryo-EM structure of Tetrahymena thermophila mitochondrial ATP synthase - F1Fo tetramer
Map dataLocal-resolution filtered full map of T. thermophila ATP synthase tetramer, Fo-subcomplexes masked
Sample
  • Complex: Mitochondrial ATP synthase, F1Fo tetramer
    • Protein or peptide: x 28 types
  • Ligand: x 9 types
Function / homology
Function and homology information


: / mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) / 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) / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / mitochondrial inner membrane ...: / mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) / 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) / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / mitochondrial inner membrane / oxidoreductase activity / hydrolase activity / lipid binding / ATP hydrolysis activity / mitochondrion / ATP binding / membrane
Similarity search - Function
Sulphide quinone-reductase / ATP synthase, F0 complex, subunit D, mitochondrial / ATP synthase D chain, mitochondrial (ATP5H) / ATP synthase, F0 complex, subunit D superfamily, mitochondrial / F1F0 ATP synthase OSCP/delta subunit, N-terminal domain superfamily / ATPase, OSCP/delta subunit / ATP synthase delta (OSCP) subunit / F1F0 ATP synthase subunit C superfamily / FAD/NAD(P)-binding domain / ATP synthase, F0 complex, subunit C, DCCD-binding site ...Sulphide quinone-reductase / ATP synthase, F0 complex, subunit D, mitochondrial / ATP synthase D chain, mitochondrial (ATP5H) / ATP synthase, F0 complex, subunit D superfamily, mitochondrial / F1F0 ATP synthase OSCP/delta subunit, N-terminal domain superfamily / ATPase, OSCP/delta subunit / ATP synthase delta (OSCP) subunit / F1F0 ATP synthase subunit C superfamily / FAD/NAD(P)-binding domain / ATP synthase, F0 complex, subunit C, DCCD-binding site / ATP synthase c subunit signature. / Pyridine nucleotide-disulphide oxidoreductase / 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 / alpha/beta hydrolase fold / 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 / Alpha/beta hydrolase fold-1 / 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 / ACP-like superfamily / Carrier protein (CP) domain profile. / Phosphopantetheine binding ACP domain / FAD/NAD(P)-binding domain superfamily / Alpha/Beta hydrolase fold / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Transmembrane protein, putative / Uncharacterized protein / Oxidoreductase, putative / Transmembrane protein / ATP synthase subunit beta / Transmembrane protein, putative / Transmembrane protein / Alpha/beta hydrolase / Uncharacterized protein / Transmembrane protein, putative ...Transmembrane protein, putative / Uncharacterized protein / Oxidoreductase, putative / Transmembrane protein / ATP synthase subunit beta / Transmembrane protein, putative / Transmembrane protein / Alpha/beta hydrolase / Uncharacterized protein / Transmembrane protein, putative / Transmembrane protein / Transmembrane protein / Uncharacterized protein / Transmembrane protein, putative / Uncharacterized protein / ATP synthase F1, delta subunit / Uncharacterized protein / Uncharacterized protein / Acyl carrier protein, putative / ATP synthase subunit gamma / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / ATP synthase subunit alpha / Transmembrane protein / Ymf56 / ATP synthase F0 subunit 9 / Ymf66
Similarity search - Component
Biological speciesTetrahymena thermophila (eukaryote)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsKock Flygaard R / Muhleip A / Amunts A
Funding support Sweden, 3 items
OrganizationGrant numberCountry
Swedish Research CouncilNT_2015-04107 Sweden
Knut and Alice Wallenberg Foundation2018.0080 Sweden
European Research Council (ERC)ERC-2018-StG-805230 Sweden
CitationJournal: Nat Commun / Year: 2020
Title: Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization.
Authors: Rasmus Kock Flygaard / Alexander Mühleip / Victor Tobiasson / Alexey Amunts /
Abstract: Mitochondrial ATP synthases form functional homodimers to induce cristae curvature that is a universal property of mitochondria. To expand on the understanding of this fundamental phenomenon, we ...Mitochondrial ATP synthases form functional homodimers to induce cristae curvature that is a universal property of mitochondria. To expand on the understanding of this fundamental phenomenon, we characterized the unique type III mitochondrial ATP synthase in its dimeric and tetrameric form. The cryo-EM structure of a ciliate ATP synthase dimer reveals an unusual U-shaped assembly of 81 proteins, including a substoichiometrically bound ATPTT2, 40 lipids, and co-factors NAD and CoQ. A single copy of subunit ATPTT2 functions as a membrane anchor for the dimeric inhibitor IF. Type III specific linker proteins stably tie the ATP synthase monomers in parallel to each other. The intricate dimer architecture is scaffolded by an extended subunit-a that provides a template for both intra- and inter-dimer interactions. The latter results in the formation of tetramer assemblies, the membrane part of which we determined to 3.1 Å resolution. The structure of the type III ATP synthase tetramer and its associated lipids suggests that it is the intact unit propagating the membrane curvature.
History
DepositionApr 14, 2020-
Header (metadata) releaseSep 30, 2020-
Map releaseSep 30, 2020-
UpdateNov 11, 2020-
Current statusNov 11, 2020Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.012
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.012
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6ynz
  • Surface level: 0.012
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-6ynz
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_10861.png

Downloads & links

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Map

FileDownload / File: emd_10861.map.gz / Format: CCP4 / Size: 824 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationLocal-resolution filtered full map of T. thermophila ATP synthase tetramer, Fo-subcomplexes masked
Voxel sizeX=Y=Z: 0.83 Å
Density
Contour LevelBy AUTHOR: 0.012 / Movie #1: 0.012
Minimum - Maximum-0.027042763 - 0.06968886
Average (Standard dev.)0.000114906354 (±0.0030414008)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions600600600
Spacing600600600
CellA=B=C: 498.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z0.830.830.83
M x/y/z600600600
origin x/y/z0.0000.0000.000
length x/y/z498.000498.000498.000
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS600600600
D min/max/mean-0.0270.0700.000

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Supplemental data

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Mask #1

Fileemd_10861_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half-map 1

Fileemd_10861_half_map_1.map
AnnotationHalf-map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half-map 2

Fileemd_10861_half_map_2.map
AnnotationHalf-map 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Mitochondrial ATP synthase, F1Fo tetramer

EntireName: Mitochondrial ATP synthase, F1Fo tetramer
Components
  • Complex: Mitochondrial ATP synthase, F1Fo tetramer
    • Protein or peptide: Ymf66
    • Protein or peptide: subunit b
    • Protein or peptide: subunit d
    • Protein or peptide: subunit f
    • Protein or peptide: subunit i/j
    • Protein or peptide: subunit k
    • Protein or peptide: Ymf56
    • Protein or peptide: ATPTT3
    • Protein or peptide: ATPTT4
    • Protein or peptide: ATPTT5
    • Protein or peptide: ATPTT6
    • Protein or peptide: ATPTT7
    • Protein or peptide: ATPTT8
    • Protein or peptide: ATPTT9
    • Protein or peptide: ATPTT10
    • Protein or peptide: ATPTT11
    • Protein or peptide: ATPTT12
    • Protein or peptide: ATPTT13
    • Protein or peptide: ATPTT1
    • Protein or peptide: Inhibitor of F1 (IF1)
    • Protein or peptide: ATPTT2
    • Protein or peptide: Oligomycin sensitivity-conferring protein (OSCP)
    • Protein or peptide: ATP synthase subunit gamma
    • Protein or peptide: ATP synthase subunit alpha
    • Protein or peptide: ATP synthase subunit beta
    • Protein or peptide: ATP synthase F0 subunit 9
    • Protein or peptide: subunit delta
    • Protein or peptide: subunit epsilon
  • Ligand: CARDIOLIPIN
  • Ligand: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
  • Ligand: PHOSPHATE IONPhosphate
  • Ligand: Ubiquinone-8Coenzyme Q10
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: 1,2-Dioleoyl-sn-glycero-3-phosphoethanolamine
  • Ligand: NICOTINAMIDE-ADENINE-DINUCLEOTIDE
  • Ligand: ADENOSINE-5'-DIPHOSPHATE

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Supramolecule #1: Mitochondrial ATP synthase, F1Fo tetramer

SupramoleculeName: Mitochondrial ATP synthase, F1Fo tetramer / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#28
Source (natural)Organism: Tetrahymena thermophila (eukaryote)

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Macromolecule #1: Ymf66

MacromoleculeName: Ymf66 / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 52.561461 KDa
SequenceString: MGRENVLPVH NDVYEDFVFT TPYFQPESTF KSVPKLFSDI LLGGVEWVYT TSESVLAYDY KLWYLWSGVS NLDESFDMFF NQYWALSLS TSVFQLFYAV ILDRYLSVLF QNTPYTNDWF RMMLHSKETA LIWLYHPELS WHINGLNQFF TYFYGGILEF V YFDKSNPD ...String:
MGRENVLPVH NDVYEDFVFT TPYFQPESTF KSVPKLFSDI LLGGVEWVYT TSESVLAYDY KLWYLWSGVS NLDESFDMFF NQYWALSLS TSVFQLFYAV ILDRYLSVLF QNTPYTNDWF RMMLHSKETA LIWLYHPELS WHINGLNQFF TYFYGGILEF V YFDKSNPD MCILVHTLWI HLLILFLIFT GFVTILFSFY GNPNTEENTI DSDYLAASGT VEAEKEITSI DDYLGLVFAI AY VFGVFFY VHGWTSMLSH AVLLLSCYSI IIMFLFILGM PTLLLYDFGI FFLAYLKGAG KYISSVAEMM FDYTACLVFY IRI LAQWIR VVLMVVTFIS LSHYVSDFDI TNSALIGSEN QSDSMNELNT NFSMTYYILT VLPGKFIYWI YEILHTFFVV CSQF VAFFA IVFWLFLFLY TFFIIEKHED FFSKKREERK KKLKELWNLK N

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Macromolecule #2: subunit b

MacromoleculeName: subunit b / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 43.910102 KDa
SequenceString: MHSTLRVFTK NNCLSFTNMN RFSTAAQVAQ ANYSKFRADY SASVAAFQQR IKTIEKENTG SMKKPMAKAY EHPYNSEHHP LNFSAVKIA ETFHDFIGPE QVSPHYESFA MSRKFLLTFW GGFFVLNFGM ATVDLNWIMK STYIPWIFWF QLMYFYVEGK N SMFMPLLQ ...String:
MHSTLRVFTK NNCLSFTNMN RFSTAAQVAQ ANYSKFRADY SASVAAFQQR IKTIEKENTG SMKKPMAKAY EHPYNSEHHP LNFSAVKIA ETFHDFIGPE QVSPHYESFA MSRKFLLTFW GGFFVLNFGM ATVDLNWIMK STYIPWIFWF QLMYFYVEGK N SMFMPLLQ RFYRRAAANE IFTMEAFYHE NIENKLRNLM RITKGQLEYW DIHTSYGEIR ADSINNFLAN EYLRLQSHIT SR ALNILKQ AQAYETMNQA ALLQKLIDDA TSAIDNALKG DKKAEVLARS LDSAIDGLSK GYMDYQNDPL LPLILSSIEA NVK KITTLS AQEQANLIGL TAEQLKSIKE NDVRARKEFL ESQPKLDNNL KNIESVKKIL ATWGK

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Macromolecule #3: subunit d

MacromoleculeName: subunit d / type: protein_or_peptide / ID: 3 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 26.747951 KDa
SequenceString: MSMLAKIAKN VVKTQALKNT TAAQTPSFQA PGNQDKILKW ISTLSNKATT GESRSYCTQL SSLVSFYNKQ HVEQIPTIDF NEWKSVIST QGLVDKVKEN YESLIKEQYN TDAISKQISS ASSKALDDIE NELSFHAAIW LNAYADYTMF LFELEEYNDP N DYLMHENF ...String:
MSMLAKIAKN VVKTQALKNT TAAQTPSFQA PGNQDKILKW ISTLSNKATT GESRSYCTQL SSLVSFYNKQ HVEQIPTIDF NEWKSVIST QGLVDKVKEN YESLIKEQYN TDAISKQISS ASSKALDDIE NELSFHAAIW LNAYADYTMF LFELEEYNDP N DYLMHENF DFFRGLETEL EELTETHNYI PGAKDDVNLR GYLATQFAWG KKVISFYRHP ADDFKCAKAT KNMLGR

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Macromolecule #4: subunit f

MacromoleculeName: subunit f / type: protein_or_peptide / ID: 4 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 24.265398 KDa
SequenceString: MSLHEKMQTD YLWVKDHSQA DSWAKARTHG YNYIAHTVPN KKERYEMIWR SMGKSTDWEL EKFRLGKKFP DRGNKRRWFK NLFRLIKNP MGYIFWKTYK ARLAKPSLIV TSMFIGFTLG FIKLKAQSIA YSKKQYATLR AGKNIEGSGQ VHFGYHDQKW G MPAIPMFQ ...String:
MSLHEKMQTD YLWVKDHSQA DSWAKARTHG YNYIAHTVPN KKERYEMIWR SMGKSTDWEL EKFRLGKKFP DRGNKRRWFK NLFRLIKNP MGYIFWKTYK ARLAKPSLIV TSMFIGFTLG FIKLKAQSIA YSKKQYATLR AGKNIEGSGQ VHFGYHDQKW G MPAIPMFQ LMYYELPGNS IVVNPCRNQN YRLYFEMRKK LGILPA

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Macromolecule #5: subunit i/j

MacromoleculeName: subunit i/j / type: protein_or_peptide / ID: 5 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 24.395543 KDa
SequenceString: MNPIQKAWLK ILEPVSYVIN EKMAKRTGII GKLGRFFAIG PREYGVHPIN RMFIFMNRKY MAFQAVALHR YSFVKSLTHN GFHMLRVFR HFAFVLPATV LAGLGLFVYW GDDNKCYSPD RFPYLKKRAG DMALPLNSLN QRTSAHYIEI NAIYGAEMMK R YHKVWENI ...String:
MNPIQKAWLK ILEPVSYVIN EKMAKRTGII GKLGRFFAIG PREYGVHPIN RMFIFMNRKY MAFQAVALHR YSFVKSLTHN GFHMLRVFR HFAFVLPATV LAGLGLFVYW GDDNKCYSPD RFPYLKKRAG DMALPLNSLN QRTSAHYIEI NAIYGAEMMK R YHKVWENI IEERSKATDQ EKKTRYAHPS YQYSPLPVVS IPNVLNPLNL Q

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Macromolecule #6: subunit k

MacromoleculeName: subunit k / type: protein_or_peptide / ID: 6 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 20.963871 KDa
SequenceString:
MWYKYFSKQS WNLRVWRKAN LKYNQDDFGM TQPKYIARFG DFRFRLVRTE GALRGCMFFV GFGCFSIINY LYGRYGYIIN ESSQKRAAQ DLLDNDMAAD KILFKNRVGA PTRPLRSLDD MMAFLSGSAT YDQLADYASY NHAMDVNQDQ QAGLDSWMSE K DKNMVKYY QRSLGKKVEG I

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Macromolecule #7: Ymf56

MacromoleculeName: Ymf56 / type: protein_or_peptide / ID: 7 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 12.299238 KDa
SequenceString:
MITILDYLFL LDLNDDLTRK AVFEQVIIFI FIYCTMNFLA WSTVVELIWP THFFNRRHSS SQEFIRFRTY TEVLLKISAY NDFFYVLNN YYYNQKLILK N

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Macromolecule #8: ATPTT3

MacromoleculeName: ATPTT3 / type: protein_or_peptide / ID: 8 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 34.719633 KDa
SequenceString: MINRSTAFIS KNLRQANLTQ SSLAMKTQYN QMGFSSDNPY NKRWEYKWKH SYYTYPRDYE HTEVRKPQDS KDVPPIYFAY YKDFVDRWL PGMNMWWQRR HRIFDKFNVY FLPGMSLFFY QFADLALGFK IMAAFPLFLA YTRIRDKTLD PDFKETYLRD M IYQNPEIT ...String:
MINRSTAFIS KNLRQANLTQ SSLAMKTQYN QMGFSSDNPY NKRWEYKWKH SYYTYPRDYE HTEVRKPQDS KDVPPIYFAY YKDFVDRWL PGMNMWWQRR HRIFDKFNVY FLPGMSLFFY QFADLALGFK IMAAFPLFLA YTRIRDKTLD PDFKETYLRD M IYQNPEIT KYFNEETIHV LDYEFEYLPG YLCPEKFPEY QNKTWQFFNT DTAQAEGFFK FGDVESGATM TLKFKTMPIP GK FRYQVGE PFYFYDLRAE IKCDGVYKEV VLVDEKESLK KIRPFLFLI

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Macromolecule #9: ATPTT4

MacromoleculeName: ATPTT4 / type: protein_or_peptide / ID: 9 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 32.484051 KDa
SequenceString: MQQRKKIYLR QKRKIYIQLK NKEKKKNNQF IQKREKMGYK IRNKSIFWTR AGWKNNWHPK NFNAPRPSYG EFTMGIRCRN DHHSFLRYV QTYRNMSRHC KQYFLGDKQL EETFILGLRS LFLVPYDSQC LTDQIKHGGE RRFVDQLDRD FELISYNTHP Y QLFTYTVR ...String:
MQQRKKIYLR QKRKIYIQLK NKEKKKNNQF IQKREKMGYK IRNKSIFWTR AGWKNNWHPK NFNAPRPSYG EFTMGIRCRN DHHSFLRYV QTYRNMSRHC KQYFLGDKQL EETFILGLRS LFLVPYDSQC LTDQIKHGGE RRFVDQLDRD FELISYNTHP Y QLFTYTVR NEHLAWKNEQ YEKIQKGEKT FEQELLDYLD EQVLAEKAKL RDGQNFSIER MTEIALHVFR KARAGKVRPA QD VRGPDGN VNDFLEQRRP FEHPNPTGVT H

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Macromolecule #10: ATPTT5

MacromoleculeName: ATPTT5 / type: protein_or_peptide / ID: 10 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 31.674639 KDa
SequenceString: MSENKAPGQI YAYDIHNTHY PYVNIKQDSQ TQLLASFRRS IASINPFSYR QVPSQDRAAF GLRWGNAWYA PNPYPNGIHF DRVFPTHYD PLAETNRTKA NLQLIKYAPG NYSTLVVTSE KLPRPCIRTI QNYRRCQMVN GTEKCNSEAQ DILAICPNWA L DHMKEKVR ...String:
MSENKAPGQI YAYDIHNTHY PYVNIKQDSQ TQLLASFRRS IASINPFSYR QVPSQDRAAF GLRWGNAWYA PNPYPNGIHF DRVFPTHYD PLAETNRTKA NLQLIKYAPG NYSTLVVTSE KLPRPCIRTI QNYRRCQMVN GTEKCNSEAQ DILAICPNWA L DHMKEKVR FYTKALAINN QTYIRAMQVE EYNQGRTVAD VAPKTWIHGT RQHLRPDTMW ADDRYTNITQ TEINEAIKRV EA RKAREHE KKPVEQANVN ANTGEQPVRV EKSLYP

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Macromolecule #11: ATPTT6

MacromoleculeName: ATPTT6 / type: protein_or_peptide / ID: 11 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 29.354383 KDa
SequenceString: MPVKEGQAKL WFSTKEEADA YDDKMISNIE LKSQDYEDEN FSPVFNRKTQ EYFLEPSEKF KSDFAELLRP LRSLSFNQVV DRYVLIPPN HTFYRNWTYE KFLGGFGLSY LILRELPLRN FYARVFVMYA FAAKVLDHLG NPFPFSGHGQ IVAAADRWNH W DVRCYDNV ...String:
MPVKEGQAKL WFSTKEEADA YDDKMISNIE LKSQDYEDEN FSPVFNRKTQ EYFLEPSEKF KSDFAELLRP LRSLSFNQVV DRYVLIPPN HTFYRNWTYE KFLGGFGLSY LILRELPLRN FYARVFVMYA FAAKVLDHLG NPFPFSGHGQ IVAAADRWNH W DVRCYDNV MKALKYIRIP TVQNNIPEAT RWYGRQPGHL LRADTYWIPN LVSQRFAKHQ PAHWDGTQNM PIFRLADPKH KD SYMVQFR

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Macromolecule #12: ATPTT7

MacromoleculeName: ATPTT7 / type: protein_or_peptide / ID: 12 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 26.355104 KDa
SequenceString: MDNYFTAITL LGLRDQNLPP FKDARLQRYK SIKKMIDLIE TTTKLAPPMP VELFMLNPTD PEWDDDMTYP TITHATALYK SSALAGNLF LYAYNYNNFT ANIRLRTMRY LFPVVSLAIF GNIYWDYRSQ LVKVNLFDEY IQARAQELVK QNEYLLEHED V KRYVWWYE ...String:
MDNYFTAITL LGLRDQNLPP FKDARLQRYK SIKKMIDLIE TTTKLAPPMP VELFMLNPTD PEWDDDMTYP TITHATALYK SSALAGNLF LYAYNYNNFT ANIRLRTMRY LFPVVSLAIF GNIYWDYRSQ LVKVNLFDEY IQARAQELVK QNEYLLEHED V KRYVWWYE DLKETLARVH RQANNHKACD FKDSEIILQD FIRRYTNPKD NLPIKFHPQG QTF

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Macromolecule #13: ATPTT8

MacromoleculeName: ATPTT8 / type: protein_or_peptide / ID: 13 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 21.782971 KDa
SequenceString:
MEGFIQNKRK KEKEGEEEEE SKEKRKQINQ LNKQKQEEEK IYQQKKDQKR KKYLYQRKEM TIFAETWEAS EYQYRNKANL KTLPVNHLG KLAELKFDFV EYKAHQLIAC HLYERMTIHC MNQYGLFKDF YRPECLDAQY YFKTCVELNA AYGIQKKFFP E HFVGSPYA RPVPQFQQLG L

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Macromolecule #14: ATPTT9

MacromoleculeName: ATPTT9 / type: protein_or_peptide / ID: 14 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 18.199361 KDa
SequenceString:
MKQKINKLLK NKGVQDKYKY LSKLILLDQE IKGKIKRKNK KEKQKRKNKL ILEEMQNTTN IVHVPVHMGH THYFDYIDSF PKLKEGPTL EENHITNQKI LREQLISGQQ GLEQNLCLRN CFKLSQKRYI EFCLDRKCGG ADFQRAATIL GYTKN

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Macromolecule #15: ATPTT10

MacromoleculeName: ATPTT10 / type: protein_or_peptide / ID: 15 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 17.425703 KDa
SequenceString:
MSNIFLELQD GDKTVYTHTS LIEESKQEQI QAIYDKVPQW TNGGRFLGFW LSMEAVNRVQ SVAKLPIYYR AGIVATSTLL GGLVSSLVF WKSGNENQVA KLANGAPVYL KKWEVPELSK LYFFLDDDNN FKPSLNHHAV TQGRQYYKIY QHN

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Macromolecule #16: ATPTT11

MacromoleculeName: ATPTT11 / type: protein_or_peptide / ID: 16 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 17.410811 KDa
SequenceString:
MFRNILSLVT KPSKLSQKTF YNFAAAKNEV QVSKKQQQAG AKRDLTQYVE GQIVNRNQLT LKKQEDIEQY VLKLVRGYFR TTNKQGLNI NSVLQDHGLD EFDSIELAMQ VEEDLGYVIS AETIPVLNKV KHFVNYINHV EQFKAENGKA PIA

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Macromolecule #17: ATPTT12

MacromoleculeName: ATPTT12 / type: protein_or_peptide / ID: 17 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 17.34382 KDa
SequenceString:
MSQDPKIVNP QLWPNPNKLR FADLYKYQGV EMKKINDSIK NYKAAKFYIG GILGGCLVFK FFIDAAVDKY IFGENGNGGK FLEMQTINS NYDYYYNRQF QRMRYLTEDP AGDDPLQKTK DEHLVDLGFI PKVFGANVEV RKRAPHDKYL

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Macromolecule #18: ATPTT13

MacromoleculeName: ATPTT13 / type: protein_or_peptide / ID: 18 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 16.81625 KDa
SequenceString:
MNSLSSKKAN SLVFKSIRNF TLQWGSLAER PMVDRVMSTS TWPVPYYQRL FKAYPIREKK DKMSLLLSDI DIDDTNWYQA KDFLRGSFR GRQIVDYVEN NIASNTYILI QQDVANMAKA YVHDICGYID VANKENVRIL SKGDLI

+
Macromolecule #19: ATPTT1

MacromoleculeName: ATPTT1 / type: protein_or_peptide / ID: 19 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 54.917816 KDa
SequenceString: MIHCLRNIRT VSALQSKISY NLGGGNKRKK TSGDLDNYDV LFVGANLGGI CSNHFDKDTH GKYKCFVSFD QPINQIYSVR IPYEQQRVR KSEYIHFSKK SINQFTPSEM LAVKEILPEQ NAVVLSSGRR IGYNQLVLAT GLKHDFSQIK GFYEALEHPE H PVYANRDP ...String:
MIHCLRNIRT VSALQSKISY NLGGGNKRKK TSGDLDNYDV LFVGANLGGI CSNHFDKDTH GKYKCFVSFD QPINQIYSVR IPYEQQRVR KSEYIHFSKK SINQFTPSEM LAVKEILPEQ NAVVLSSGRR IGYNQLVLAT GLKHDFSQIK GFYEALEHPE H PVYANRDP ETWRSAQHKY SKYISNFKSG DGYFCIPEYP YAGEVECFNF FVSDEVWKWA QHHGALSPKH TFTIVNANEK FV HYCDSAD AFIKERLEKR GIRVEYNTKL LEVHQDGQKA TFINTKTGEK SVRDYNNLYS IVPSKRQEFL DKAGLTNGNG LLN VDHQTL QHKKYKNIFG LGDAADLPTT KTFWAGWYQI AVVRNNVKRN LQGQTLNAHY DGFSKVPLFT GHQTLTYVAH SYGG VGNWQ HLKHNNGGIL AWMRYRSWAK GMAKKFQDFY NGARLGPPYH KVLKSFPELP GSPESQQSSG ISKYFPTKTE NKAAH

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Macromolecule #20: Inhibitor of F1 (IF1)

MacromoleculeName: Inhibitor of F1 (IF1) / type: protein_or_peptide / ID: 20 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 12.987691 KDa
SequenceString:
MNRSVNIAKN LIQTYRAMSV QSRFAFSTRE EEWLDKRTKS QEKVYFDQED RKAMKRLLEK LNTTSKFVED SEYLAPQNLE VENILKRYH INYTQALIDE LVDWKTGKN

+
Macromolecule #21: ATPTT2

MacromoleculeName: ATPTT2 / type: protein_or_peptide / ID: 21 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 54.34468 KDa
SequenceString: MKMEYLQSEE KKDAINKQIH KKEEKEEKEI KIKRKNKVKQ RIQIINQIKK YIEAKQQKKQ IQSKNQRKYK GRMINTRKQV FKCLWGAQP AYNFSRIINH LRGDPVYQDN TKDVSLRGTF LRGKYDDLPT MIFFTEACDL TANWIPFFTN PQYDILAHRN V WLLNPRNF ...String:
MKMEYLQSEE KKDAINKQIH KKEEKEEKEI KIKRKNKVKQ RIQIINQIKK YIEAKQQKKQ IQSKNQRKYK GRMINTRKQV FKCLWGAQP AYNFSRIINH LRGDPVYQDN TKDVSLRGTF LRGKYDDLPT MIFFTEACDL TANWIPFFTN PQYDILAHRN V WLLNPRNF GNSDRHPSFD LQEMSDDVMR FMYSQKISMA TLGGHGIGGK IALAVGCYHA ERVTGVFSID SSPMDQRYHE AF KEFKGYV NALTEINFKT WSDKDVKVFL KENIKDPKWR SIFTNNISKN AKTQSDSFNF EINYLNHNLN FNKADSLGNW AVK NGIYTG RAHFIFPEYS RWVHLATNTL PMHKVCARVK GFGHDIFYVQ GDENPLNHWV YDFENYANVV ASKLNKFLHS YDGV HALLK DRTEIGNFMI PDRIKSRNDS KHIYGDYSPA HLHHNWRFNH IYEKHDELDK KLNEQ

+
Macromolecule #22: Oligomycin sensitivity-conferring protein (OSCP)

MacromoleculeName: Oligomycin sensitivity-conferring protein (OSCP) / type: protein_or_peptide / ID: 22 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 24.782355 KDa
SequenceString: MQVIRKHLAQ KGLFNPFLFN RFSTQQDITS VPGDKPPAIE DSIHGKYAGV LFSSASSNKS LNKVAEDMKY FNQLYKESEV FKSFLNNVS LKRNQQRDII SALGKTNFNP ATNNLLETLI ENKRLDSLPK IAEKYMDYYR ILNKQESITI ISAQELTAAE K QKVEQGLK ...String:
MQVIRKHLAQ KGLFNPFLFN RFSTQQDITS VPGDKPPAIE DSIHGKYAGV LFSSASSNKS LNKVAEDMKY FNQLYKESEV FKSFLNNVS LKRNQQRDII SALGKTNFNP ATNNLLETLI ENKRLDSLPK IAEKYMDYYR ILNKQESITI ISAQELTAAE K QKVEQGLK KGNANVQFTV VYQVDPAILG GLQMYSGNNF LDCSLLSRVN KLKTEIAKIS F

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Macromolecule #23: ATP synthase subunit gamma

MacromoleculeName: ATP synthase subunit gamma / type: protein_or_peptide / ID: 23 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 32.915152 KDa
SequenceString: MFGLASKGFI NTSLVMVPQM NFGANLKQLK IRMKAIGSIK KITKAMKMVA ASKMKAETSR LENGRNFAVG SVQKMLENES YVQKKKSTT APKSTLLVPI TSDKGLCGSV NSSIVREVKR LALNNRSAFG LLPVGEKGSS GLSRPFPDLL KSSIVNIQNV N FPTAAAIA ...String:
MFGLASKGFI NTSLVMVPQM NFGANLKQLK IRMKAIGSIK KITKAMKMVA ASKMKAETSR LENGRNFAVG SVQKMLENES YVQKKKSTT APKSTLLVPI TSDKGLCGSV NSSIVREVKR LALNNRSAFG LLPVGEKGSS GLSRPFPDLL KSSIVNIQNV N FPTAAAIA HQVSTQGAGY DQVTLIYNHF KNAISYVVKH QELLPRAQFL NLFKYVTRHE AVEPELEYSK NYFFELYMAS SV YNALLNS SASEQASRMN AMENASKNAG EILSKLTLDY NKARQAKITM ELIEIISGAS IV

+
Macromolecule #24: ATP synthase subunit alpha

MacromoleculeName: ATP synthase subunit alpha / type: protein_or_peptide / ID: 24 / Number of copies: 12 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 59.744012 KDa
SequenceString: MIRNFHSLVK RVPRLALTPF FGFRTSMTLA DKKLSTGEAS VVLAEKIKGI TQQNDITEYG TVISIGDGIA RVFGLTKVQA GEMVEFKSG IRGMALNLET DNVGVVVLGN DRDIKEGDVV KRTGAIVDVP IGEAMCGRVF DALGNPIDGL GPLKTTQRAR V EIKAPGII ...String:
MIRNFHSLVK RVPRLALTPF FGFRTSMTLA DKKLSTGEAS VVLAEKIKGI TQQNDITEYG TVISIGDGIA RVFGLTKVQA GEMVEFKSG IRGMALNLET DNVGVVVLGN DRDIKEGDVV KRTGAIVDVP IGEAMCGRVF DALGNPIDGL GPLKTTQRAR V EIKAPGII PRQSVRQPMQ TGIKCVDSLV PIGRGQRELI IGDRQTGKTA IAIDTILNQK EAFNTGDVKK QLYCIYVAVG QK RSTIANL VSILKQHDCM KFTIVVCATA SDAAPLQFLA PYSGCAIGEF FRDNGKHALI IYDDLSKQAV AYRQMSLLLR RPP GREAYP GDVFYLHSRL LERAAKMNDS LGGGSLTALP VIETQAGDVS AYIPTNVISI TDGQIFLETE LFYKGIRPAI NVGL SVSRV GSAAQIKAMK KIAGNLKLTL ATYRELAAFS QFGSDLDAKT QQQLNTGERL VEMLKQNQYT PMKVEEQVCI IFAGV KGFL DALVTSEVLK FEKKFLEHVR TNHSALLKRI RDSGDLSEVD TNELNTIIPL FIQEGGFKLK AQ

+
Macromolecule #25: ATP synthase subunit beta

MacromoleculeName: ATP synthase subunit beta / type: protein_or_peptide / ID: 25 / Number of copies: 12 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 53.490848 KDa
SequenceString: MLSKALQRGI ARAFSTTAKK EAPKTVKANG QVSQVIGAVV DVQFEGELPQ ILNALEVQGT QHRLVLEVAQ HLGDSRVRTI AMDSTEGLV RGQPVVDTGL PISVPVGPGT LGRIMNVIGE PIDQRGPIKA AKLYPIHRDA PSFTDQATSA EILVTGIKVV D LLAPYARG ...String:
MLSKALQRGI ARAFSTTAKK EAPKTVKANG QVSQVIGAVV DVQFEGELPQ ILNALEVQGT QHRLVLEVAQ HLGDSRVRTI AMDSTEGLV RGQPVVDTGL PISVPVGPGT LGRIMNVIGE PIDQRGPIKA AKLYPIHRDA PSFTDQATSA EILVTGIKVV D LLAPYARG GKIGLFGGAG VGKTVLIQEL INNVAKHHGG YSVFAGVGER TREGNDLYHE MMDSKVISVK EGESRCALIF GQ MNEPPGA RARVGLTGLT VAEYFRDEEG KDVLLFVDNI FRFTQACSEV SALLGRIPSA VGYQPTLATD LGALQERITT TQK GSITSV QAIYVPADDL TDPAPATTFA HLDATTVLNR GLTELGIYPA VDPLDSTSRM LDPITIGEEH YTVARGVQKL LQDY KSLQD IIAILGVDDL SEEDKLVVAR ARKVQKFLSQ PFFMSEVFSG IPGRFVNLKQ NIASFKALLE GAGDEYPESC FYMKG DLEE SLAAGRADAL KSK

+
Macromolecule #26: ATP synthase F0 subunit 9

MacromoleculeName: ATP synthase F0 subunit 9 / type: protein_or_peptide / ID: 26 / Number of copies: 40 / Enantiomer: LEVO / EC number: ec: 3.6.1.34
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 8.083702 KDa
SequenceString:
MLLVKAVKVL VMGGCMLPIA FGALGTGVLF AGFNVALSRN PEETESLFNN TLMGFALIET FIFMSIGLGF FVLFAA

+
Macromolecule #27: subunit delta

MacromoleculeName: subunit delta / type: protein_or_peptide / ID: 27 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 17.892537 KDa
SequenceString:
MFTRFVTQPT LLTQTQRALF SALTKKQKME VTLRTPYKEY LANFDGFSRI TAKTNEASLV IQNKTPASLY VLPPGPLKIR FTSEVKNVS GDFLHTGGWV IVHADNTCEI NVMDLFDRKE VRADQFEKGN IQDLDTLAGK YAAKSRKSTV RLFTKATTQ

+
Macromolecule #28: subunit epsilon

MacromoleculeName: subunit epsilon / type: protein_or_peptide / ID: 28 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Tetrahymena thermophila (eukaryote)
Molecular weightTheoretical: 7.986336 KDa
SequenceString:
MCIEFAFKKA GIPIVRNFLH STEGVIYGLP QRVQRNLAIN YTVKQYKEGK AVSAKTIKTL QEAFPSKGDT K

+
Macromolecule #29: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 29 / Number of copies: 60 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM / Cardiolipin

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Macromolecule #30: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE

MacromoleculeName: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / type: ligand / ID: 30 / Number of copies: 12 / Formula: PC1
Molecular weightTheoretical: 790.145 Da
Chemical component information

ChemComp-PC1:
1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM / Phosphatidylcholine

+
Macromolecule #31: PHOSPHATE ION

MacromoleculeName: PHOSPHATE ION / type: ligand / ID: 31 / Number of copies: 4 / Formula: PO4
Molecular weightTheoretical: 94.971 Da
Chemical component information

ChemComp-PO4:
PHOSPHATE ION / Phosphate

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Macromolecule #32: Ubiquinone-8

MacromoleculeName: Ubiquinone-8 / type: ligand / ID: 32 / Number of copies: 4 / Formula: UQ8
Molecular weightTheoretical: 727.109 Da
Chemical component information

ChemComp-UQ8:
Ubiquinone-8

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Macromolecule #33: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 33 / Number of copies: 16 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

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

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Macromolecule #34: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 34 / Number of copies: 24 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #35: 1,2-Dioleoyl-sn-glycero-3-phosphoethanolamine

MacromoleculeName: 1,2-Dioleoyl-sn-glycero-3-phosphoethanolamine / type: ligand / ID: 35 / Number of copies: 8 / Formula: PEE
Molecular weightTheoretical: 749.073 Da
Chemical component information

ChemComp-PEE:
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE, phospholipid*YM / Discrete optimized protein energy

+
Macromolecule #36: NICOTINAMIDE-ADENINE-DINUCLEOTIDE

MacromoleculeName: NICOTINAMIDE-ADENINE-DINUCLEOTIDE / type: ligand / ID: 36 / Number of copies: 4 / Formula: NAD
Molecular weightTheoretical: 663.425 Da
Chemical component information

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM / Nicotinamide adenine dinucleotide

+
Macromolecule #37: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 37 / Number of copies: 8 / 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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Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.75 mg/mL
BufferpH: 7.5
GridModel: Quantifoil R2/2 / Material: COPPER / Mesh: 300
VitrificationCryogen name: ETHANE / 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 opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 165000
Specialist opticsEnergy filter - Name: GIF Quantum LS / Energy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: COUNTING / Average electron dose: 30.9 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

CTF correctionSoftware - Name: CTFFIND (ver. 4.1.13)
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1) / Software - details: beta
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1) / Software - details: beta
Final reconstructionApplied symmetry - Point group: C2 (2 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.1) / Software - details: beta / Number images used: 40691
FSC plot (resolution estimation)

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