+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-26825 | |||||||||
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Title | Citrus V-ATPase State 1, H in contact with subunit a | |||||||||
Map data | ||||||||||
Sample |
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Keywords | V-ATPase / rotary ATPase / complex / MEMBRANE PROTEIN | |||||||||
Function / homology | Function and homology information proton-transporting V-type ATPase, V1 domain / proton-transporting V-type ATPase, V0 domain / proton-transporting two-sector ATPase complex, catalytic domain / vacuolar proton-transporting V-type ATPase, V0 domain / vacuolar proton-transporting V-type ATPase, V1 domain / proton-transporting V-type ATPase complex / vacuolar acidification / vacuole / vacuolar membrane / ATP metabolic process ...proton-transporting V-type ATPase, V1 domain / proton-transporting V-type ATPase, V0 domain / proton-transporting two-sector ATPase complex, catalytic domain / vacuolar proton-transporting V-type ATPase, V0 domain / vacuolar proton-transporting V-type ATPase, V1 domain / proton-transporting V-type ATPase complex / vacuolar acidification / vacuole / vacuolar membrane / ATP metabolic process / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / transmembrane transport / ATP hydrolysis activity / ATP binding / membrane Similarity search - Function | |||||||||
Biological species | Citrus limon (lemon) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.2 Å | |||||||||
Authors | Keon KA / Abdelaziz RA / Schulze WX / Schumacher K / Rubinstein JL | |||||||||
Funding support | Canada, 1 items
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Citation | Journal: Structure / Year: 2022 Title: 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. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_26825.map.gz | 94.2 MB | EMDB map data format | |
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Header (meta data) | emd-26825-v30.xml emd-26825.xml | 30.7 KB 30.7 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_26825_fsc.xml | 9.9 KB | Display | FSC data file |
Images | emd_26825.png | 62.5 KB | ||
Filedesc metadata | emd-26825.cif.gz | 8.2 KB | ||
Others | emd_26825_additional_1.map.gz emd_26825_half_map_1.map.gz emd_26825_half_map_2.map.gz | 97.4 MB 95.6 MB 95.6 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-26825 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-26825 | HTTPS FTP |
-Validation report
Summary document | emd_26825_validation.pdf.gz | 900 KB | Display | EMDB validaton report |
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Full document | emd_26825_full_validation.pdf.gz | 899.6 KB | Display | |
Data in XML | emd_26825_validation.xml.gz | 18.2 KB | Display | |
Data in CIF | emd_26825_validation.cif.gz | 23.5 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-26825 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-26825 | HTTPS FTP |
-Related structure data
Related structure data | 7uw9MC 7uwaC 7uwbC 7uwcC 7uwdC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_26825.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
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: #1
File | emd_26825_additional_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_26825_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_26825_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
+Entire : Citrus V-ATPase
+Supramolecule #1: Citrus V-ATPase
+Macromolecule #1: V-type proton ATPase subunit H
+Macromolecule #2: V-type proton ATPase catalytic subunit A
+Macromolecule #3: V-type proton ATPase subunit B2
+Macromolecule #4: V-type proton ATPase subunit D
+Macromolecule #5: V-type proton ATPase subunit F
+Macromolecule #6: V-type proton ATPase subunit AP1 fragment
+Macromolecule #7: V-type proton ATPase subunit c"
+Macromolecule #8: V-type proton ATPase subunit d2
+Macromolecule #9: V-type proton ATPase subunit c
+Macromolecule #10: V-type proton ATPase subunit AP2 fragment
+Macromolecule #11: V-type proton ATPase subunit E
+Macromolecule #12: V-type proton ATPase subunit G
+Macromolecule #13: V-type proton ATPase subunit C
+Macromolecule #14: V-type proton ATPase subunit a3
+Macromolecule #15: V-type proton ATPase subunit e1
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
-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 |