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Yorodumi- EMDB-4640: Thermus thermophilus V/A-type ATPase/synthase, rotational state 1 -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-4640 | |||||||||
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Title | Thermus thermophilus V/A-type ATPase/synthase, rotational state 1 | |||||||||
Map data | A combined map from focused refinements of several domains of the intact complex as described in the paper. | |||||||||
Sample |
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Keywords | ATP hydrolysis/synthesis / proton translocation / rotary catalysis / MEMBRANE PROTEIN | |||||||||
Function / homology | Function and homology information proton-transporting V-type ATPase, V0 domain / proton-transporting two-sector ATPase complex, catalytic domain / proton-transporting ATP synthase complex / proton motive force-driven plasma membrane ATP synthesis / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / ATP binding / metal ion binding Similarity search - Function | |||||||||
Biological species | Thermus thermophilus HB8 (bacteria) / Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.25 Å | |||||||||
Authors | Zhou L / Sazanov L | |||||||||
Citation | Journal: Science / Year: 2019 Title: Structure and conformational plasticity of the intact V/A-type ATPase. Authors: Long Zhou / Leonid A Sazanov / Abstract: V (vacuolar)/A (archaeal)-type adenosine triphosphatases (ATPases), found in archaea and eubacteria, couple ATP hydrolysis or synthesis to proton translocation across the plasma membrane using the ...V (vacuolar)/A (archaeal)-type adenosine triphosphatases (ATPases), found in archaea and eubacteria, couple ATP hydrolysis or synthesis to proton translocation across the plasma membrane using the rotary-catalysis mechanism. They belong to the V-type ATPase family, which differs from the mitochondrial/chloroplast F-type ATP synthases in overall architecture. We solved cryo-electron microscopy structures of the intact V/A-ATPase, reconstituted into lipid nanodiscs, in three rotational states and two substates. These structures indicate substantial flexibility between V and V in a working enzyme, which results from mechanical competition between central shaft rotation and resistance from the peripheral stalks. We also describe details of adenosine diphosphate inhibition release, V-V torque transmission, and proton translocation, which are relevant for the entire V-type ATPase family. | |||||||||
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_4640.map.gz | 3.3 MB | EMDB map data format | |
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Header (meta data) | emd-4640-v30.xml emd-4640.xml | 35.8 KB 35.8 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_4640_fsc.xml | 17 KB | Display | FSC data file |
Images | emd_4640.png | 163.2 KB | ||
Filedesc metadata | emd-4640.cif.gz | 8.2 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-4640 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-4640 | HTTPS FTP |
-Validation report
Summary document | emd_4640_validation.pdf.gz | 455.7 KB | Display | EMDB validaton report |
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Full document | emd_4640_full_validation.pdf.gz | 455.2 KB | Display | |
Data in XML | emd_4640_validation.xml.gz | 4.4 KB | Display | |
Data in CIF | emd_4640_validation.cif.gz | 4.9 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-4640 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-4640 | HTTPS FTP |
-Related structure data
Related structure data | 6qumMC 4699C 4700C 4702C 4703C 6r0wC 6r0yC 6r0zC 6r10C 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_4640.map.gz / Format: CCP4 / Size: 16.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | A combined map from focused refinements of several domains of the intact complex as described in the paper. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. generated in cubic-lattice coordinate | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.085 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
+Entire : Thermus thermophilus V/A-type ATPase/ATP synthase
+Supramolecule #1: Thermus thermophilus V/A-type ATPase/ATP synthase
+Macromolecule #1: V-type ATP synthase alpha chain
+Macromolecule #2: V-type ATP synthase beta chain
+Macromolecule #3: V-type ATP synthase subunit D
+Macromolecule #4: V-type ATP synthase subunit F
+Macromolecule #5: V-type ATP synthase, subunit (VAPC-THERM)
+Macromolecule #6: V-type ATP synthase subunit E
+Macromolecule #7: V-type ATP synthase subunit C
+Macromolecule #8: V-type ATP synthase subunit I
+Macromolecule #9: V-type ATP synthase, subunit K
+Macromolecule #10: MAGNESIUM ION
+Macromolecule #11: ADENOSINE-5'-DIPHOSPHATE
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 5.4 mg/mL | |||||||||||||||
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Buffer | pH: 8 Component:
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Grid | Model: Quantifoil R0.6/1 / Material: COPPER / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 120 sec. | |||||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Number grids imaged: 1 / Number real images: 2700 / Average exposure time: 63.0 sec. / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Calibrated defocus max: 1.78 µm / Calibrated defocus min: 0.5 µm / Calibrated magnification: 129032 / Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 75000 |
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 / Overall B value: 91.2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Output model | PDB-6qum: |