+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-11195 | |||||||||
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Title | bovine ATP synthase rotor domain, state 1 | |||||||||
Map data | Rotor state1 main map | |||||||||
Sample |
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Function / homology | Function and homology information Formation of ATP by chemiosmotic coupling / Cristae formation / mitochondrial proton-transporting ATP synthase complex assembly / mitochondrial envelope / proton-transporting ATP synthase complex / : / : / Mitochondrial protein degradation / proton motive force-driven ATP synthesis / proton motive force-driven mitochondrial ATP synthesis ...Formation of ATP by chemiosmotic coupling / Cristae formation / mitochondrial proton-transporting ATP synthase complex assembly / mitochondrial envelope / proton-transporting ATP synthase complex / : / : / Mitochondrial protein degradation / proton motive force-driven ATP synthesis / proton motive force-driven mitochondrial ATP synthesis / proton transmembrane transporter activity / proton-transporting ATP synthase activity, rotational mechanism / aerobic respiration / proton transmembrane transport / mitochondrial inner membrane / lipid binding / mitochondrion Similarity search - Function | |||||||||
Biological species | Bos taurus (cattle) / Bovine (cattle) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.49 Å | |||||||||
Authors | Spikes T / Montgomery MG / Walker JE | |||||||||
Funding support | United Kingdom, 2 items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2020 Title: Structure of the dimeric ATP synthase from bovine mitochondria. Authors: Tobias E Spikes / Martin G Montgomery / John E Walker / Abstract: The structure of the dimeric ATP synthase from bovine mitochondria determined in three rotational states by electron cryo-microscopy provides evidence that the proton uptake from the mitochondrial ...The structure of the dimeric ATP synthase from bovine mitochondria determined in three rotational states by electron cryo-microscopy provides evidence that the proton uptake from the mitochondrial matrix via the proton inlet half channel proceeds via a Grotthus mechanism, and a similar mechanism may operate in the exit half channel. The structure has given information about the architecture and mechanical constitution and properties of the peripheral stalk, part of the membrane extrinsic region of the stator, and how the action of the peripheral stalk damps the side-to-side rocking motions that occur in the enzyme complex during the catalytic cycle. It also describes wedge structures in the membrane domains of each monomer, where the skeleton of each wedge is provided by three α-helices in the membrane domains of the b-subunit to which the supernumerary subunits e, f, and g and the membrane domain of subunit A6L are bound. Protein voids in the wedge are filled by three specifically bound cardiolipin molecules and two other phospholipids. The external surfaces of the wedges link the monomeric complexes together into the dimeric structures and provide a pivot to allow the monomer-monomer interfaces to change during catalysis and to accommodate other changes not related directly to catalysis in the monomer-monomer interface that occur in mitochondrial cristae. The structure of the bovine dimer also demonstrates that the structures of dimeric ATP synthases in a tetrameric porcine enzyme have been seriously misinterpreted in the membrane domains. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_11195.map.gz | 440.3 MB | EMDB map data format | |
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Header (meta data) | emd-11195-v30.xml emd-11195.xml | 21.9 KB 21.9 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_11195_fsc.xml | 17.7 KB | Display | FSC data file |
Images | emd_11195.png | 45.6 KB | ||
Masks | emd_11195_msk_1.map | 476.8 MB | Mask map | |
Others | emd_11195_half_map_1.map.gz emd_11195_half_map_2.map.gz | 383.3 MB 383.2 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-11195 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-11195 | HTTPS FTP |
-Validation report
Summary document | emd_11195_validation.pdf.gz | 317.6 KB | Display | EMDB validaton report |
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Full document | emd_11195_full_validation.pdf.gz | 316.7 KB | Display | |
Data in XML | emd_11195_validation.xml.gz | 22.7 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-11195 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-11195 | HTTPS FTP |
-Related structure data
Related structure data | 6zg7MC 6yy0C 6z1rC 6z1uC 6zbbC 6zg8C 6zikC 6ziqC 6zitC 6ziuC 6zmrC 6znaC 6zpoC 6zqmC 6zqnC C: citing same article (ref.) M: atomic model generated by this map |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_11195.map.gz / Format: CCP4 / Size: 476.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Rotor state1 main map | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.048 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
File | emd_11195_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: Rotor state1 half map 1
File | emd_11195_half_map_1.map | ||||||||||||
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Annotation | Rotor state1 half map 1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Rotor state1 half map 2
File | emd_11195_half_map_2.map | ||||||||||||
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Annotation | Rotor state1 half map 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Bovine ATP synthase
Entire | Name: Bovine ATP synthase |
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Components |
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-Supramolecule #1: Bovine ATP synthase
Supramolecule | Name: Bovine ATP synthase / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Bos taurus (cattle) |
Molecular weight | Experimental: 7.441 KDa |
-Macromolecule #1: ATP synthase subunit gamma, mitochondrial
Macromolecule | Name: ATP synthase subunit gamma, mitochondrial / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Bovine (cattle) |
Molecular weight | Theoretical: 30.30076 KDa |
Sequence | String: ATLKDITRRL KSIKNIQKIT KSMKMVAAAK YARAERELKP ARVYGVGSLA LYEKADIKTP EDKKKHLIIG VSSDRGLCGA IHSSVAKQM KSEAANLAAA GKEVKIIGVG DKIRSILHRT HSDQFLVTFK EVGRRPPTFG DASVIALELL NSGYEFDEGS I IFNRFRSV ...String: ATLKDITRRL KSIKNIQKIT KSMKMVAAAK YARAERELKP ARVYGVGSLA LYEKADIKTP EDKKKHLIIG VSSDRGLCGA IHSSVAKQM KSEAANLAAA GKEVKIIGVG DKIRSILHRT HSDQFLVTFK EVGRRPPTFG DASVIALELL NSGYEFDEGS I IFNRFRSV ISYKTEEKPI FSLDTISSAE SMSIYDDIDA DVLRNYQEYS LANIIYYSLK ESTTSEQSAR MTAMDNASKN AS EMIDKLT LTFNRTRQAV ITKELIEIIS GAAALD |
-Macromolecule #2: ATP synthase subunit delta, mitochondrial
Macromolecule | Name: ATP synthase subunit delta, mitochondrial / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Bovine (cattle) |
Molecular weight | Theoretical: 15.074813 KDa |
Sequence | String: AEAAAAQAPA AGPGQMSFTF ASPTQVFFNS ANVRQVDVPT QTGAFGILAA HVPTLQVLRP GLVVVHAEDG TTSKYFVSSG SVTVNADSS VQLLAEEAVT LDMLDLGAAK ANLEKAQSEL LGAADEATRA EIQIRIEANE ALVKALE |
-Macromolecule #3: ATP synthase subunit epsilon, mitochondrial
Macromolecule | Name: ATP synthase subunit epsilon, mitochondrial / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Bovine (cattle) |
Molecular weight | Theoretical: 5.662693 KDa |
Sequence | String: VAYWRQAGLS YIRYSQICAK AVRDALKTEF KANAMKTSGS TIKIVKVKKE |
-Macromolecule #4: ATP synthase F(0) complex subunit C2, mitochondrial
Macromolecule | Name: ATP synthase F(0) complex subunit C2, mitochondrial / type: protein_or_peptide / ID: 4 / Number of copies: 8 / Enantiomer: LEVO |
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Source (natural) | Organism: Bovine (cattle) |
Molecular weight | Theoretical: 7.653034 KDa |
Sequence | String: DIDTAAKFIG AGAATVGVAG SGAGIGTVFG SLIIGYARNP SL(M3L)QQLFSYA ILGFALSEAM GLFCLMVAFL ILFAM |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 4.5 mg/mL |
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Buffer | pH: 7.4 |
Vitrification | Cryogen 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.. |
Details | Nickel affinity purified filled by gel filtration |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film 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 beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
+Image processing
-Atomic model buiding 1
Initial model |
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Refinement | Space: REAL / Protocol: RIGID BODY FIT | ||||||||||||||||||||||||
Output model | PDB-6zg7: |