+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-8462 | |||||||||
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Title | Thermus thermophilus V/A-ATPase bound to VH dAbs | |||||||||
Map data | Thermus thermophilus V/A-ATPase bound to VH dAb | |||||||||
Sample |
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Keywords | V/A-ATPase / membrane protein / complex / antibody / HYDROLASE | |||||||||
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 | Homo sapiens (human) / Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 8.7 Å | |||||||||
Authors | Davies RB / Smits C / Wong ASW / Stock D / Sandin S / Stewart AG | |||||||||
Funding support | Australia, 2 items
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Citation | Journal: J Struct Biol / Year: 2017 Title: Cryo-EM analysis of a domain antibody bound rotary ATPase complex. Authors: Roberta B Davies / Callum Smits / Andrew S W Wong / Daniela Stock / Mary Christie / Sara Sandin / Alastair G Stewart / Abstract: The bacterial A/V-type ATPase/synthase rotary motor couples ATP hydrolysis/synthesis with proton translocation across biological membranes. The A/V-type ATPase/synthase from Thermus thermophilus has ...The bacterial A/V-type ATPase/synthase rotary motor couples ATP hydrolysis/synthesis with proton translocation across biological membranes. The A/V-type ATPase/synthase from Thermus thermophilus has been extensively studied both structurally and functionally for many years. Here we provide an 8.7Å resolution cryo-electron microscopy 3D reconstruction of this complex bound to single-domain antibody fragments, small monomeric antibodies containing just the variable heavy domain. Docking of known structures into the density revealed the molecular orientation of the domain antibodies, suggesting that structure determination of co-domain antibody:protein complexes could be a useful avenue for unstable or smaller proteins. Although previous studies suggested that the presence of fluoroaluminate in this complex could change the rotary state of this enzyme, we observed no gross structural rearrangements under these conditions. | |||||||||
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_8462.map.gz | 19.4 MB | EMDB map data format | |
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Header (meta data) | emd-8462-v30.xml emd-8462.xml | 20.9 KB 20.9 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_8462_fsc.xml | 6.2 KB | Display | FSC data file |
Images | emd_8462.png | 56.8 KB | ||
Filedesc metadata | emd-8462.cif.gz | 7.3 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-8462 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-8462 | HTTPS FTP |
-Validation report
Summary document | emd_8462_validation.pdf.gz | 511.1 KB | Display | EMDB validaton report |
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Full document | emd_8462_full_validation.pdf.gz | 510.7 KB | Display | |
Data in XML | emd_8462_validation.xml.gz | 9 KB | Display | |
Data in CIF | emd_8462_validation.cif.gz | 11.6 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-8462 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-8462 | HTTPS FTP |
-Related structure data
Related structure data | 5tsjMC M: atomic model generated by this map C: citing same article (ref.) |
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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_8462.map.gz / Format: CCP4 / Size: 21.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Thermus thermophilus V/A-ATPase bound to VH dAb | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.91 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-ATPase bound to VH dAbs
+Supramolecule #1: Thermus thermophilus V/A-ATPase bound to VH dAbs
+Macromolecule #1: V-type ATP synthase alpha chain
+Macromolecule #2: V-type ATP synthase beta chain
+Macromolecule #3: V-type ATP synthase subunit E
+Macromolecule #4: V-type ATPase subunit G
+Macromolecule #5: V-type ATP synthase subunit D
+Macromolecule #6: V-type ATP synthase subunit F
+Macromolecule #7: V-type ATP synthase subunit C
+Macromolecule #8: Archaeal/vacuolar-type H+-ATPase subunit I
+Macromolecule #9: Vacuolar type ATP synthase subunit
+Macromolecule #10: Human heavy chain domain antibody
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TALOS ARCTICA |
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Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Average electron dose: 13.8 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Talos Arctica / Image courtesy: FEI Company |
+Image processing
-Atomic model buiding 1
Refinement | Protocol: RIGID BODY FIT |
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Output model | PDB-5tsj: |