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- EMDB-10859: Cryo-EM structure of Tetrahymena thermophila mitochondrial ATP sy... -

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Basic information

Entry
Database: EMDB / ID: EMD-10859
TitleCryo-EM structure of Tetrahymena thermophila mitochondrial ATP synthase - Fo-subcomplex
Map dataLocal-resolution filtered full map of T. thermophila ATP synthase Fo-subcomplex
Sample
  • Complex: Mitochondrial ATP synthase, Fo-subcomplex
    • Protein or peptide: x 21 types
  • Ligand: x 8 types
Function / homology
Function and homology information


mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) / proton motive force-driven ATP synthesis / proton transmembrane transporter activity / oxidoreductase activity / hydrolase activity / mitochondrion / 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 / FAD/NAD(P)-binding domain / Pyridine nucleotide-disulphide oxidoreductase / alpha/beta hydrolase fold / Alpha/beta hydrolase fold-1 / ACP-like superfamily / Carrier protein (CP) domain profile. ...Sulphide quinone-reductase / ATP synthase, F0 complex, subunit D, mitochondrial / ATP synthase D chain, mitochondrial (ATP5H) / ATP synthase, F0 complex, subunit D superfamily, mitochondrial / FAD/NAD(P)-binding domain / Pyridine nucleotide-disulphide oxidoreductase / alpha/beta hydrolase fold / Alpha/beta hydrolase fold-1 / ACP-like superfamily / Carrier protein (CP) domain profile. / Phosphopantetheine binding ACP domain / FAD/NAD(P)-binding domain superfamily / Alpha/Beta hydrolase fold
Similarity search - Domain/homology
Transmembrane protein, putative / Uncharacterized protein / Oxidoreductase, putative / Transmembrane protein / Transmembrane protein, putative / Transmembrane protein / Alpha/beta hydrolase / Uncharacterized protein / Transmembrane protein, putative / Transmembrane protein ...Transmembrane protein, putative / Uncharacterized protein / Oxidoreductase, putative / Transmembrane protein / Transmembrane protein, putative / Transmembrane protein / Alpha/beta hydrolase / Uncharacterized protein / Transmembrane protein, putative / Transmembrane protein / Transmembrane protein / Uncharacterized protein / Transmembrane protein, putative / Uncharacterized protein / Uncharacterized protein / Acyl carrier protein, putative / Uncharacterized protein / Uncharacterized protein / Transmembrane protein / Ymf56 / Ymf66
Similarity search - Component
Biological speciesTetrahymena thermophila (eukaryote)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.5 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: 0.02
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.02
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6ynx
  • Surface level: 0.02
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-6ynx
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_10859.png

Downloads & links

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Map

FileDownload / File: emd_10859.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 Fo-subcomplex
Voxel sizeX=Y=Z: 0.83 Å
Density
Contour LevelBy AUTHOR: 0.018 / Movie #1: 0.02
Minimum - Maximum-0.055942725 - 0.1592571
Average (Standard dev.)0.00029939073 (±0.0032668915)
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-0.0560.1590.000

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Supplemental data

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Mask #1

Fileemd_10859_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half-map 2

Fileemd_10859_half_map_1.map
AnnotationHalf-map 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half-map 1

Fileemd_10859_half_map_2.map
AnnotationHalf-map 1
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, Fo-subcomplex

EntireName: Mitochondrial ATP synthase, Fo-subcomplex
Components
  • Complex: Mitochondrial ATP synthase, Fo-subcomplex
    • Protein or peptide: subunit a
    • 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: subunit 8
    • 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
  • 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

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Supramolecule #1: Mitochondrial ATP synthase, Fo-subcomplex

SupramoleculeName: Mitochondrial ATP synthase, Fo-subcomplex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#21
Source (natural)Organism: Tetrahymena thermophila (eukaryote)

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Macromolecule #1: subunit a

MacromoleculeName: subunit a / type: protein_or_peptide / ID: 1 / Number of copies: 2 / 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: 2 / 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: 2 / 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: 2 / 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: 2 / 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: 2 / 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: subunit 8

MacromoleculeName: subunit 8 / type: protein_or_peptide / ID: 7 / Number of copies: 2 / 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: 2 / 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: 2 / 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: 2 / 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: 2 / 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: 2 / 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: 2 / 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: 2 / 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: 2 / 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: 2 / 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: 2 / 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: 2 / 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

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Macromolecule #19: ATPTT1

MacromoleculeName: ATPTT1 / type: protein_or_peptide / ID: 19 / Number of copies: 2 / 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: 2 / 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

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Macromolecule #21: ATPTT2

MacromoleculeName: ATPTT2 / type: protein_or_peptide / ID: 21 / Number of copies: 1 / 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

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Macromolecule #22: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 22 / Number of copies: 30 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM / Cardiolipin

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Macromolecule #23: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE

MacromoleculeName: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / type: ligand / ID: 23 / Number of copies: 6 / Formula: PC1
Molecular weightTheoretical: 790.145 Da
Chemical component information

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

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Macromolecule #24: PHOSPHATE ION

MacromoleculeName: PHOSPHATE ION / type: ligand / ID: 24 / Number of copies: 2 / Formula: PO4
Molecular weightTheoretical: 94.971 Da
Chemical component information

ChemComp-PO4:
PHOSPHATE ION / Phosphate

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Macromolecule #25: Ubiquinone-8

MacromoleculeName: Ubiquinone-8 / type: ligand / ID: 25 / Number of copies: 2 / Formula: UQ8
Molecular weightTheoretical: 727.109 Da
Chemical component information

ChemComp-UQ8:
Ubiquinone-8

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Macromolecule #26: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 26 / Number of copies: 2 / 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 #27: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 27 / Number of copies: 2 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #28: 1,2-Dioleoyl-sn-glycero-3-phosphoethanolamine

MacromoleculeName: 1,2-Dioleoyl-sn-glycero-3-phosphoethanolamine / type: ligand / ID: 28 / Number of copies: 4 / 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

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Macromolecule #29: NICOTINAMIDE-ADENINE-DINUCLEOTIDE

MacromoleculeName: NICOTINAMIDE-ADENINE-DINUCLEOTIDE / type: ligand / ID: 29 / Number of copies: 2 / Formula: NAD
Molecular weightTheoretical: 663.425 Da
Chemical component information

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

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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

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

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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: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 2.5 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.1) / Software - details: beta / Number images used: 61157
FSC plot (resolution estimation)

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