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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Citrus V-ATPase State 2, Highest-Resolution Class | |||||||||
Map data | Citrus V-ATPase State 2, Highest-Resolution Class | |||||||||
Sample |
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Keywords | V-ATPase / rotary ATPase / complex / MEMBRANE PROTEIN | |||||||||
| Function / homology | Function and homology informationproton-transporting V-type ATPase, V1 domain / proton-transporting two-sector ATPase complex, catalytic domain / proton-transporting V-type ATPase, V0 domain / vacuolar proton-transporting V-type ATPase, V1 domain / vacuolar proton-transporting V-type ATPase, V0 domain / proton-transporting V-type ATPase complex / plant-type vacuole / vacuole / vacuolar acidification / vacuolar membrane ...proton-transporting V-type ATPase, V1 domain / proton-transporting two-sector ATPase complex, catalytic domain / proton-transporting V-type ATPase, V0 domain / vacuolar proton-transporting V-type ATPase, V1 domain / vacuolar proton-transporting V-type ATPase, V0 domain / proton-transporting V-type ATPase complex / plant-type vacuole / vacuole / vacuolar acidification / vacuolar membrane / proton-transporting ATPase activity, rotational mechanism / H+-transporting two-sector ATPase / ATP metabolic process / endomembrane system / transmembrane transport / ATPase binding / ATP hydrolysis activity / ATP binding / membrane Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.9 Å | |||||||||
Authors | Tan YZ / Rubinstein JL | |||||||||
| Funding support | Canada, 1 items
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Citation | Journal: Structure / Year: 2022Title: Structure of V-ATPase from citrus fruit. Authors: Yong Zi Tan / Kristine A Keon / Rana Abdelaziz / Peter Imming / Waltraud Schulze / Karin Schumacher / John L Rubinstein / ![]() Abstract: We used the Legionella pneumophila effector SidK to affinity purify the endogenous vacuolar-type ATPases (V-ATPases) from lemon fruit. The preparation was sufficient for cryoelectron microscopy, ...We used the Legionella pneumophila effector SidK to affinity purify the endogenous vacuolar-type ATPases (V-ATPases) from lemon fruit. The preparation was sufficient for cryoelectron microscopy, allowing structure determination of the enzyme in two rotational states. The structure defines the ATP:H ratio of the enzyme, demonstrating that it can establish a maximum ΔpH of ∼3, which is insufficient to maintain the low pH observed in the vacuoles of juice sac cells in lemons and other citrus fruit. Compared with yeast and mammalian enzymes, the membrane region of the plant V-ATPase lacks subunit f and possesses an unusual configuration of transmembrane α helices. Subunit H, which inhibits ATP hydrolysis in the isolated catalytic region of V-ATPase, adopts two different conformations in the intact complex, hinting at a role in modulating activity in the intact enzyme. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_26827.map.gz | 13.8 MB | EMDB map data format | |
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| Header (meta data) | emd-26827-v30.xml emd-26827.xml | 31 KB 31 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_26827_fsc.xml | 10.4 KB | Display | FSC data file |
| Images | emd_26827.png | 55.7 KB | ||
| Filedesc metadata | emd-26827.cif.gz | 8.2 KB | ||
| Others | emd_26827_additional_1.map.gz emd_26827_half_map_1.map.gz emd_26827_half_map_2.map.gz | 97.4 MB 95.6 MB 95.6 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-26827 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-26827 | HTTPS FTP |
-Validation report
| Summary document | emd_26827_validation.pdf.gz | 858.8 KB | Display | EMDB validaton report |
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| Full document | emd_26827_full_validation.pdf.gz | 858.4 KB | Display | |
| Data in XML | emd_26827_validation.xml.gz | 16.8 KB | Display | |
| Data in CIF | emd_26827_validation.cif.gz | 20.9 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-26827 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-26827 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 7uwbMC ![]() 7uw9C ![]() 7uwaC ![]() 7uwcC ![]() 7uwdC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_26827.map.gz / Format: CCP4 / Size: 15 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Citrus V-ATPase State 2, Highest-Resolution Class | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. generated in cubic-lattice coordinate | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.617 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: Citrus V-ATPase State 2, Highest-Resolution Class
| File | emd_26827_additional_1.map | ||||||||||||
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| Annotation | Citrus V-ATPase State 2, Highest-Resolution Class | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: Citrus V-ATPase State 2, Highest-Resolution Class
| File | emd_26827_half_map_1.map | ||||||||||||
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| Annotation | Citrus V-ATPase State 2, Highest-Resolution Class | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: Citrus V-ATPase State 2, Highest-Resolution Class
| File | emd_26827_half_map_2.map | ||||||||||||
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| Annotation | Citrus V-ATPase State 2, Highest-Resolution Class | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
+Entire : Citrus V-ATPase
+Supramolecule #1: Citrus V-ATPase
+Macromolecule #1: V-type proton ATPase catalytic subunit A
+Macromolecule #2: V-type proton ATPase subunit B2
+Macromolecule #3: V-type proton ATPase subunit E
+Macromolecule #4: V-type proton ATPase subunit G
+Macromolecule #5: V-type proton ATPase subunit D
+Macromolecule #6: V-type proton ATPase subunit F
+Macromolecule #7: V-type proton ATPase subunit C
+Macromolecule #8: V-type proton ATPase subunit H
+Macromolecule #9: V-type proton ATPase subunit a3
+Macromolecule #10: V-type proton ATPase subunit AP1 fragment
+Macromolecule #11: V-type proton ATPase subunit c"
+Macromolecule #12: V-type proton ATPase subunit d2
+Macromolecule #13: V-type proton ATPase subunit e1
+Macromolecule #14: V-type proton ATPase subunit c
+Macromolecule #15: V-type proton ATPase subunit AP2 fragment
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.4 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 31.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.414211 µm / Nominal defocus min: 0.677558 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Authors
Canada, 1 items
Citation













Z (Sec.)
Y (Row.)
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Processing
FIELD EMISSION GUN

