[English] 日本語
Yorodumi
- EMDB-11430: bovine ATP synthase dimer, state1:state3 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-11430
Titlebovine ATP synthase dimer, state1:state3
Map dataATP synthase dimer state1:state3 main map
Sample
  • Complex: Bovine ATP synthase
    • Complex: monomeric bovine ATP synthase
      • Protein or peptide: x 15 types
    • Complex: Bovine ATP synthase
      • Protein or peptide: x 3 types
Function / homology
Function and homology information


angiostatin binding / Formation of ATP by chemiosmotic coupling / Cristae formation / ATPase inhibitor activity / mitochondrial proton-transporting ATP synthase complex assembly / mitochondrial envelope / negative regulation of hydrolase activity / proton-transporting ATP synthase complex / heme biosynthetic process / mitochondrial proton-transporting ATP synthase, catalytic core ...angiostatin binding / Formation of ATP by chemiosmotic coupling / Cristae formation / ATPase inhibitor activity / mitochondrial proton-transporting ATP synthase complex assembly / mitochondrial envelope / negative regulation of hydrolase activity / proton-transporting ATP synthase complex / heme biosynthetic process / mitochondrial proton-transporting ATP synthase, catalytic core / mitochondrial proton-transporting ATP synthase, stator stalk / mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) / Mitochondrial protein degradation / proton-transporting ATP synthase complex, coupling factor F(o) / mitochondrial proton-transporting ATP synthase complex / negative regulation of endothelial cell proliferation / proton motive force-driven ATP synthesis / proton transmembrane transporter activity / proton motive force-driven mitochondrial ATP synthesis / proton-transporting ATP synthase complex, catalytic core F(1) / H+-transporting two-sector ATPase / proton transmembrane transport / aerobic respiration / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / erythrocyte differentiation / ADP binding / ATPase binding / protein homotetramerization / mitochondrial inner membrane / calmodulin binding / lipid binding / structural molecule activity / cell surface / protein homodimerization activity / ATP hydrolysis activity / protein-containing complex / mitochondrion / ATP binding / identical protein binding / plasma membrane
Similarity search - Function
ATP synthase membrane subunit K / ATP synthase regulation / ATP synthase, F0 complex, subunit G, mitochondrial / ATP synthase, F0 complex, subunit E, mitochondrial / ATP synthase subunit ATP5MJ, mitochondrial / Mitochondrial ATP synthase subunit g, animal / Mitochondrial ATP synthase g subunit / ATP synthase E chain / Mitochondrial proteolipid / ATP synthase protein 8, metazoa ...ATP synthase membrane subunit K / ATP synthase regulation / ATP synthase, F0 complex, subunit G, mitochondrial / ATP synthase, F0 complex, subunit E, mitochondrial / ATP synthase subunit ATP5MJ, mitochondrial / Mitochondrial ATP synthase subunit g, animal / Mitochondrial ATP synthase g subunit / ATP synthase E chain / Mitochondrial proteolipid / ATP synthase protein 8, metazoa / Mitochondrial 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 delta/epsilon subunit, C-terminal domain superfamily / ATP synthase, F0 complex, subunit B/MI25 / ATP synthase, F0 complex, subunit B / Mitochondrial ATP synthase B chain precursor (ATP-synt_B) / ATP synthase, F0 complex, subunit D, mitochondrial / ATP synthase D chain, mitochondrial (ATP5H) / ATP synthase, F0 complex, subunit D superfamily, mitochondrial / ATP synthase, F0 complex, subunit A, bacterial/mitochondria / ATP synthase, F1 complex, epsilon subunit, mitochondrial / ATP synthase, F1 complex, epsilon subunit superfamily, mitochondrial / Mitochondrial ATP synthase epsilon chain / ATPase, OSCP/delta subunit, conserved site / ATP synthase delta (OSCP) subunit signature. / F1F0 ATP synthase OSCP/delta subunit, N-terminal domain superfamily / ATP synthase, F0 complex, subunit A / ATP synthase, F0 complex, subunit A, active site / ATP synthase, F0 complex, subunit A superfamily / ATP synthase A chain / ATP synthase a subunit signature. / ATPase, OSCP/delta subunit / ATP synthase delta (OSCP) subunit / ATP synthase, F1 complex, delta/epsilon subunit / ATP synthase, F1 complex, delta/epsilon subunit, N-terminal / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase, Delta/Epsilon chain, beta-sandwich domain / ATP synthase, F0 complex, subunit C / F1F0 ATP synthase subunit C superfamily / ATP synthase, F0 complex, subunit C, DCCD-binding site / ATP synthase c subunit signature. / ATP synthase, F1 complex, gamma subunit conserved site / ATP synthase gamma subunit signature. / ATP synthase, F1 complex, beta subunit / ATP synthase, alpha subunit, C-terminal domain superfamily / ATP synthase, F1 complex, gamma subunit / ATP synthase, F1 complex, gamma subunit superfamily / ATP synthase / ATP synthase, alpha subunit, C-terminal / ATP synthase, F1 complex, alpha subunit / ATP synthase, F1 complex, alpha subunit nucleotide-binding domain / ATP synthase alpha/beta chain, C terminal domain / V-ATPase proteolipid subunit C-like domain / F/V-ATP synthase subunit C superfamily / ATP synthase subunit C / ATPase, F1/V1 complex, beta/alpha subunit, C-terminal / ATP synthase subunit alpha, N-terminal domain-like superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain / ATP synthase alpha/beta family, beta-barrel domain / ATPase, alpha/beta subunit, nucleotide-binding domain, active site / ATP synthase alpha and beta subunits signature. / ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain / ATP synthase alpha/beta family, nucleotide-binding domain / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ATP synthase subunit beta, mitochondrial / ATP synthase subunit a / ATPase inhibitor, mitochondrial / ATP synthase-coupling factor 6, mitochondrial / ATP synthase protein 8 / ATP synthase subunit delta, mitochondrial / ATP synthase subunit gamma, mitochondrial / ATP synthase subunit epsilon, mitochondrial / ATP synthase F(0) complex subunit C2, mitochondrial / ATP synthase F(0) complex subunit B1, mitochondrial ...ATP synthase subunit beta, mitochondrial / ATP synthase subunit a / ATPase inhibitor, mitochondrial / ATP synthase-coupling factor 6, mitochondrial / ATP synthase protein 8 / ATP synthase subunit delta, mitochondrial / ATP synthase subunit gamma, mitochondrial / ATP synthase subunit epsilon, mitochondrial / ATP synthase F(0) complex subunit C2, mitochondrial / ATP synthase F(0) complex subunit B1, mitochondrial / ATP synthase subunit d, mitochondrial / ATP synthase subunit O, mitochondrial / ATP synthase subunit ATP5MJ, mitochondrial / ATP synthase subunit alpha, mitochondrial / ATP synthase subunit e, mitochondrial / ATP synthase subunit f, mitochondrial / ATP synthase subunit g, mitochondrial / ATP synthase membrane subunit K, mitochondrial
Similarity search - Component
Biological speciesBos taurus (cattle)
Methodsingle particle reconstruction / cryo EM / Resolution: 9.0 Å
AuthorsSpikes TE / Montgomery MG / Walker JE
Funding support United Kingdom, 2 items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom)MR/M009858/1 United Kingdom
Medical Research Council (MRC, United Kingdom)MC_U105663150 United Kingdom
CitationJournal: Proc Natl Acad Sci U S A / Year: 2021
Title: Interface mobility between monomers in dimeric bovine ATP synthase participates in the ultrastructure of inner mitochondrial membranes.
Authors: Tobias E Spikes / Martin G Montgomery / John E Walker /
Abstract: The ATP synthase complexes in mitochondria make the ATP required to sustain life by a rotary mechanism. Their membrane domains are embedded in the inner membranes of the organelle, and they dimerize ...The ATP synthase complexes in mitochondria make the ATP required to sustain life by a rotary mechanism. Their membrane domains are embedded in the inner membranes of the organelle, and they dimerize via interactions between their membrane domains. The dimers form extensive chains along the tips of the cristae with the two rows of monomeric catalytic domains extending into the mitochondrial matrix at an angle to each other. Disruption of the interface between dimers by mutation affects the morphology of the cristae severely. By analysis of particles of purified dimeric bovine ATP synthase by cryo-electron microscopy, we have shown that the angle between the central rotatory axes of the monomeric complexes varies between ca. 76 and 95°. These particles represent active dimeric ATP synthase. Some angular variations arise directly from the catalytic mechanism of the enzyme, and others are independent of catalysis. The monomer-monomer interaction is mediated mainly by j subunits attached to the surface of wedge-shaped protein-lipid structures in the membrane domain of the complex, and the angular variation arises from rotational and translational changes in this interaction, and combinations of both. The structures also suggest how the dimeric ATP synthases might be interacting with each other to form the characteristic rows along the tips of the cristae via other interwedge contacts, molding themselves to the range of oligomeric arrangements observed by tomography of mitochondrial membranes, and at the same time allowing the ATP synthase to operate under the range of physiological conditions that influence the structure of the cristae.
History
DepositionJul 21, 2020-
Header (metadata) releaseFeb 3, 2021-
Map releaseFeb 3, 2021-
UpdateFeb 24, 2021-
Current statusFeb 24, 2021Processing site: PDBe / Status: Released

-
Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.0129
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 0.0129
  • Imaged by UCSF Chimera
  • Download
  • Surface view with fitted model
  • Atomic models: PDB-7ajd
  • Surface level: 0.0129
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_11430.png

Downloads & links

-
Map

FileDownload / File: emd_11430.map.gz / Format: CCP4 / Size: 476.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationATP synthase dimer state1:state3 main map
Voxel sizeX=Y=Z: 1.048 Å
Density
Contour LevelBy AUTHOR: 0.0129 / Movie #1: 0.0129
Minimum - Maximum-0.01597405 - 0.042138208
Average (Standard dev.)0.0001343303 (±0.0024299002)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions500500500
Spacing500500500
CellA=B=C: 524.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0481.0481.048
M x/y/z500500500
origin x/y/z0.0000.0000.000
length x/y/z524.000524.000524.000
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ300300300
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS500500500
D min/max/mean-0.0160.0420.000

-
Supplemental data

-
Mask #1

Fileemd_11430_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Half map: ATP synthase dimer state1:state3 half map 2

Fileemd_11430_half_map_1.map
AnnotationATP synthase dimer state1:state3 half map 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Half map: ATP synthase dimer state1:state3 half map 1

Fileemd_11430_half_map_2.map
AnnotationATP synthase dimer state1:state3 half map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Sample components

+
Entire : Bovine ATP synthase

EntireName: Bovine ATP synthase
Components
  • Complex: Bovine ATP synthase
    • Complex: monomeric bovine ATP synthase
      • Protein or peptide: ATP synthase beta subunit
      • Protein or peptide: ATP synthase gamma subunit
      • Protein or peptide: ATP synthase delta subunit
      • Protein or peptide: ATP synthase epsilon subunit
      • Protein or peptide: ATP synthase a subunit
      • Protein or peptide: ATP synthase b subunit
      • Protein or peptide: ATP synthase c subunit
      • Protein or peptide: ATP synthase d subunit
      • Protein or peptide: ATP synthase e subunit
      • Protein or peptide: ATP synthase f subunit
      • Protein or peptide: ATP synthase g subunit
      • Protein or peptide: ATP synthase F6/h subunit
      • Protein or peptide: ATP synthase j subunit (6.8PL)
      • Protein or peptide: ATP synthase OSCP subunit
      • Protein or peptide: ATP synthase A6L/ATP8 subunit
    • Complex: Bovine ATP synthase
      • Protein or peptide: ATP synthase alpha subunit
      • Protein or peptide: ATP synthase k subunit (DAPIT)
      • Protein or peptide: ATP synthase inhibitor protein IF1

+
Supramolecule #1: Bovine ATP synthase

SupramoleculeName: Bovine ATP synthase / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all / Details: bovine ATP synthase inhibited by IF1 1-60His
Molecular weightExperimental: 7.441 KDa

+
Supramolecule #2: monomeric bovine ATP synthase

SupramoleculeName: monomeric bovine ATP synthase / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #2-#14, #16-#17
Details: monomeric bovine ATP synthase inhibited by IF1 1-60His
Source (natural)Organism: Bos taurus (cattle)

+
Supramolecule #3: Bovine ATP synthase

SupramoleculeName: Bovine ATP synthase / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #1, #15, #18
Source (natural)Organism: Bos taurus (cattle)
Recombinant expressionOrganism: Escherichia coli (E. coli)

+
Macromolecule #1: ATP synthase alpha subunit

MacromoleculeName: ATP synthase alpha subunit / type: protein_or_peptide / ID: 1
Details: alpha-subunit residue 1 Residue GLN 1 of chains A, B, C is not an expression tag. Again the uniprot database is misleading. The DNA sequence for this protein encodes GLU. The actual residue ...Details: alpha-subunit residue 1 Residue GLN 1 of chains A, B, C is not an expression tag. Again the uniprot database is misleading. The DNA sequence for this protein encodes GLU. The actual residue is pyroGLU. However pyroGLU and pyroGLN are the same. Residue 481 in chains A, B, and C can be Gly or SER. e.g. in this structure should be GLY. We have seen SER in some of our previous structures of bovine F1-ATPase. We have used the following REMARK in other PDB files: REMARK 999 SEQUENCE REMARK 999 RESIDUE NUMBERING: BY CONVENTION, THE REMARK 999 FIFTH AMINO ACID (SERINE) IN THE BETA SUBUNITS (CHAINS D,E,F) IS REMARK 999 RESIDUE 1 AND THE FIRST FOUR AMINO ACIDS ARE NUMBERED -4 TO -1. REMARK 999 REFERENCE FOR THE ALPHA SUBUNIT J. E. WALKER, S. J. REMARK 999 POWELL,O. VINAS AND M. J. RUNSWICK, BIOCHEMISTRY,VOL 28,PP REMARK 999 4702-4708, 1989. REMARK 999 REMARK 999 SER 481 GLY IN CHAINS A, B AND C REMARK 999 WAS IDENTIFIED AS A GLY FROM THE PROTEIN REMARK 999 SEQUENCE. IN THE CDNA SEQUENCE, THE CODON FOR THIS REMARK 999 RESIDUE WAS AGC SER IN THREE CLONES WHILE IN TWO REMARK 999 OTHERS IT WAS GGC GLY. THE DIFFERENCE WAS THOUGHT TO REMARK 999 BE DUE TO A MUTATION OCCURRING DURING EITHER PROPAGATION REMARK 999 OF THE CLONES IN THE LIBRARY OR SUBCLONING INTO M13 REMARK 999 VECTORS. THE ELECTRON DENSITY SUGGESTS A GLY IN REMARK 999 THIS POSITION.
Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
SequenceString: EKTGTAEVSS ILEERILGAD TSVDLEETGR VLSIGDGIAR VHGLRNVQAE EMVEFSSGLK GMSLNLEPD NVGVVVFGND KLIKEGDIVK RTGAIVDVPV GEELLGRVVD ALGNAIDGKG P IGSKARRR VGLKAPGIIP RISVREPMQT GIKAVDSLVP IGRGQRELII ...String:
EKTGTAEVSS ILEERILGAD TSVDLEETGR VLSIGDGIAR VHGLRNVQAE EMVEFSSGLK GMSLNLEPD NVGVVVFGND KLIKEGDIVK RTGAIVDVPV GEELLGRVVD ALGNAIDGKG P IGSKARRR VGLKAPGIIP RISVREPMQT GIKAVDSLVP IGRGQRELII GDRQTGKTSI AI DTIINQK RFNDGTDEKK KLYCIYVAIG QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAA PLQYLA PYSGCSMGEY FRDNGKHALI IYDDLSKQAV AYRQMSLLLR RPPGREAYPG DVFY LHSRL LERAAKMNDA FGGGSLTALP VIETQAGDVS AYIPTNVISI TDGQIFLETE LFYKG IRPA INVGLSVSRV GSAAQTRAMK QVAGTMKLEL AQYREVAAFA QFGSDLDAAT QQLLSR GVR LTELLKQGQY SPMAIEEQVA VIYAGVRGYL DKLEPSKITK FENAFLSHVI SQHQALL SK IRTDGKISEE SDAKLKEIVT NFLAGFEA

+
Macromolecule #2: ATP synthase beta subunit

MacromoleculeName: ATP synthase beta subunit / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
SequenceString: AAQASPSPKA GATTGRIVAV IGAVVDVQFD EGLPPILNAL EVQGRETRLV LEVAQHLGES TVRTIAMDG TEGLVRGQKV LDSGAPIRIP VGPETLGRIM NVIGEPIDER GPIKTKQFAA I HAEAPEFV EMSVEQEILV TGIKVVDLLA PYAKGGKIGL FGGAGVGKTV ...String:
AAQASPSPKA GATTGRIVAV IGAVVDVQFD EGLPPILNAL EVQGRETRLV LEVAQHLGES TVRTIAMDG TEGLVRGQKV LDSGAPIRIP VGPETLGRIM NVIGEPIDER GPIKTKQFAA I HAEAPEFV EMSVEQEILV TGIKVVDLLA PYAKGGKIGL FGGAGVGKTV LIMELINNVA KA HGGYSVF AGVGERTREG NDLYHEMIES GVINLKDATS KVALVYGQMN EPPGARARVA LTG LTVAEY FRDQEGQDVL LFIDNIFRFT QAGSEVSALL GRIPSAVGYQ PTLATDMGTM QERI TTTKK GSITSVQAIY VPADDLTDPA PATTFAHLDA TTVLSRAIAE LGIYPAVDPL DSTSR IMDP NIVGSEHYDV ARGVQKILQD YKSLQDIIAI LGMDELSEED KLTVSRARKI QRFLSQ PFQ VAEVFTGHLG KLVPLKETIK GFQQILAGEY DHLPEQAFYM VGPIEEAVAK ADKLAEE HS

+
Macromolecule #3: ATP synthase gamma subunit

MacromoleculeName: ATP synthase gamma subunit / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
SequenceString: ATLKDITRRL KSIKNIQKIT KSMKMVAAAK YARAE RELK PARVYGVGSL ALYEKADIKT PEDKKKHLII GVSSDRGLCG AIHSSVAKQM KSEAAN LAA AGKEVKIIGV GDKIRSILHR THSDQFLVTF KEVGRRPPTF GDASVIALEL LNSGYEF DE GSIIFNRFRS ...String:
ATLKDITRRL KSIKNIQKIT KSMKMVAAAK YARAE RELK PARVYGVGSL ALYEKADIKT PEDKKKHLII GVSSDRGLCG AIHSSVAKQM KSEAAN LAA AGKEVKIIGV GDKIRSILHR THSDQFLVTF KEVGRRPPTF GDASVIALEL LNSGYEF DE GSIIFNRFRS VISYKTEEKP IFSLDTISSA ESMSIYDDID ADVLRNYQEY SLANIIYY S LKESTTSEQS ARMTAMDNAS KNASEMIDKL TLTFNRTRQA VITKELIEII SGAAALD

+
Macromolecule #4: ATP synthase delta subunit

MacromoleculeName: ATP synthase delta subunit / type: protein_or_peptide / ID: 4 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
SequenceString:
AEAAAAQAPA AGPGQMSFTF ASPTQVFFNS ANVRQVDVPT QTGAFGILAA HVPTLQVLR PGLVVVHAED GTTSKYFVSS GSVTVNADSS VQLLAEEAVT L DMLDLGAA KANLEKAQSE LLGAADEATR AEIQIRIEAN EALVKALE

+
Macromolecule #5: ATP synthase epsilon subunit

MacromoleculeName: ATP synthase epsilon subunit / type: protein_or_peptide / ID: 5 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
SequenceString:
VAYWRQAGLS YIRYSQICAK AVRDALKTEF KANAMKTSGS TIKIVKVKKE

+
Macromolecule #6: ATP synthase a subunit

MacromoleculeName: ATP synthase a subunit / type: protein_or_peptide / ID: 6 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
SequenceString: MNENLFTSFI TPVILGLPL V TLIVLFPS LL FPTSNRL VSN RFVTLQ QWML QLVSK QMMSI HNSK GQTWTL MLM SLILFIG ST NLLGLLPH S FTPTTQLSM NLGMAIPLWA GAVITGFRN K TKASLAHF LP QGTPTPL IPM LVIIET ISLF IQPMA ...String:
MNENLFTSFI TPVILGLPL V TLIVLFPS LL FPTSNRL VSN RFVTLQ QWML QLVSK QMMSI HNSK GQTWTL MLM SLILFIG ST NLLGLLPH S FTPTTQLSM NLGMAIPLWA GAVITGFRN K TKASLAHF LP QGTPTPL IPM LVIIET ISLF IQPMA LAVRL TANI TAGHLL IHL IGGATLA LM SISTTTAL I TFTILILLT ILEFAVAMIQ AYVFTLLVS L YLHDNT

+
Macromolecule #7: ATP synthase b subunit

MacromoleculeName: ATP synthase b subunit / type: protein_or_peptide / ID: 7 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
SequenceString: PVPPLPEHGG KVRFGLIPE E FFQFLYPK TG VTGPYVL GTG LILYLL SKEI YVITP ETFSA ISTI GFLVYI VKK YGASVGE FA DKLNEQKI A QLEEVKQAS IKQIQDAIDM EKSQQALVQ K RHYLFDVQ RN NIAMALE VTY RERLHR VYRE VKNRL ...String:
PVPPLPEHGG KVRFGLIPE E FFQFLYPK TG VTGPYVL GTG LILYLL SKEI YVITP ETFSA ISTI GFLVYI VKK YGASVGE FA DKLNEQKI A QLEEVKQAS IKQIQDAIDM EKSQQALVQ K RHYLFDVQ RN NIAMALE VTY RERLHR VYRE VKNRL DYHIS VQNM MRQKEQ EHM INWVEKR VV QSISAQQE K ETIAKCIAD LKLLSKKAQA QPVM

+
Macromolecule #8: ATP synthase c subunit

MacromoleculeName: ATP synthase c subunit / type: protein_or_peptide / ID: 8
Details: Residue 43 is trimethylated. A post translational modification.
Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
SequenceString:
DIDTAAKFIG AGAATVGVAG SGAGIGTVFG SLIIGYARNP SL(M3L)QQLFSYA ILGFALSEA MGLFCLMVAF LILFAM

+
Macromolecule #9: ATP synthase d subunit

MacromoleculeName: ATP synthase d subunit / type: protein_or_peptide / ID: 9 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
SequenceString:
AGRKLALKTI DWVAFGEII P RNQKAVAN SL KSWNETL TSR LATLPE KPPA IDWAY YKANV AKAG LVDDFE KKF NALKVPI PE DKYTAQVD A EEKEDVKSC AEFLTQSKTR IQEYEKELE K MRNIIPFD QM TIEDLNE VFP ETKLDK KKYP YWPHR PIETL

+
Macromolecule #10: ATP synthase e subunit

MacromoleculeName: ATP synthase e subunit / type: protein_or_peptide / ID: 10 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
SequenceString:
VPPVQVSPLI KLGRYSALF L GMAYGAKR YN YLKPRAE EER RLAAEE KKKR DEQKR IEREL AEAQ EDTILK

+
Macromolecule #11: ATP synthase f subunit

MacromoleculeName: ATP synthase f subunit / type: protein_or_peptide / ID: 11 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
SequenceString:
ASVVPLKEKK LLEVKLGELP SWILMRDFTP SGIAGAFQRG YYRYYNKYV NVKKGSIAGL SMVLAAYVFL NYCRSYKELK HERLRKYH

+
Macromolecule #12: ATP synthase g subunit

MacromoleculeName: ATP synthase g subunit / type: protein_or_peptide / ID: 12 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
SequenceString:
AEFVRNLAEK APALVNAAV T YSKPRLAT FW YYAKVEL VPP TPAEIP TAIQ SLKKI INSAK TGSF KQLTVK EAL LNGLVAT EV WMWFYVGE I IGKRGIIGY DV

+
Macromolecule #13: ATP synthase F6/h subunit

MacromoleculeName: ATP synthase F6/h subunit / type: protein_or_peptide / ID: 13 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
SequenceString:
NKELDPVQKL FVDKIREYR T KRQTSGGP VD AGPEYQQ DLD RELFKL KQMY GKADM NTFPN FTFE DPKFEV VEK PQS

+
Macromolecule #14: ATP synthase j subunit (6.8PL)

MacromoleculeName: ATP synthase j subunit (6.8PL) / type: protein_or_peptide / ID: 14 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
SequenceString:
MLQSLIKKVW IPMKPYYTQ A YQEIWVGT GL MAYIVYK IRS ADKRSK ALKA SSAAP AHGHH

+
Macromolecule #15: ATP synthase k subunit (DAPIT)

MacromoleculeName: ATP synthase k subunit (DAPIT) / type: protein_or_peptide / ID: 15 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
SequenceString:
AGPEADAQF HFTGIKKYFN SYTLTGRMN C VLATYGSI AL IVLYFKL RSK KTPAVK AT

+
Macromolecule #16: ATP synthase OSCP subunit

MacromoleculeName: ATP synthase OSCP subunit / type: protein_or_peptide / ID: 16 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
SequenceString: FAKLVRPPVQ IYGIEGRYA T ALYSAASK QN KLEQVEK ELL RVGQIL KEPK MAASL LNPYV KRSV KVKSLS DMT AKEKFSP LT SNLINLLA E NGRLTNTPA VISAFSTMMS VHRGEVPCT V TTASALDE AT LTELKTV LKS FLSKGQ VLKL EVKID ...String:
FAKLVRPPVQ IYGIEGRYA T ALYSAASK QN KLEQVEK ELL RVGQIL KEPK MAASL LNPYV KRSV KVKSLS DMT AKEKFSP LT SNLINLLA E NGRLTNTPA VISAFSTMMS VHRGEVPCT V TTASALDE AT LTELKTV LKS FLSKGQ VLKL EVKID PSIMG GMIV RIGEKY VDM SAKTKIQ KL SRAMREIL

+
Macromolecule #17: ATP synthase A6L/ATP8 subunit

MacromoleculeName: ATP synthase A6L/ATP8 subunit / type: protein_or_peptide / ID: 17 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
SequenceString:
MPQLDTSTWL TMILSMFLT L FIIFQLKV SK HNFYHNP ELT PTKMLK QNTP WETKW TKIYL PLLL PL

+
Macromolecule #18: ATP synthase inhibitor protein IF1

MacromoleculeName: ATP synthase inhibitor protein IF1 / type: protein_or_peptide / ID: 18 / Details: Residues 1-60 of IF1 with a 6His tag / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (cattle)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
GSESGDNVRS SAGAVRDAGG AFGKREQAEE ERYFRARAKE QLAALKKHHE NEISHHAKE IHHHHHH

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

Concentration4.5 mg/mL
BufferpH: 7.4
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 294 K / Instrument: FEI VITROBOT MARK IV
Details: The sample was allowed to penetrate through the holey support and to distribute to both sides of the grid surface for ca. 15 sec. Then the grids were blotted with filter paper for 8-10 sec before blotting..
DetailsNickel affinity purified filled by gel filtration

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: COUNTING / Average exposure time: 12.0 sec. / Average electron dose: 4.6 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

CTF correctionSoftware: (Name: RELION (ver. 3.1), CTFFIND (ver. 4.1))
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

2v7q

Final reconstructionResolution.type: BY AUTHOR / Resolution: 9.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.1) / Number images used: 12721
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1)
Final 3D classificationSoftware - Name: RELION (ver. 3.1)
FSC plot (resolution estimation)

-
Atomic model buiding 1

Initial model
PDB IDChain

2v7q

chain_id: A

2v7q

chain_id: B

2v7q

chain_id: C

2v7q

chain_id: D

2v7q

chain_id: E

2v7q

chain_id: F

2v7q

chain_id: G

2v7q

chain_id: H

2v7q

chain_id: I

2v7q

chain_id: J

2cly

chain_id: A

2cly

chain_id: B

2cly

chain_id: C
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-7ajd:
bovine ATP synthase dimer state1:state3

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbjlvh1.pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more