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- EMDB-27987: YAR027W and YAR028W in complex with c subunits from yeast VO complex -
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Open data
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Basic information
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Title | YAR027W and YAR028W in complex with c subunits from yeast VO complex | |||||||||
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Biological species | ![]() ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 5.7 Å | |||||||||
![]() | Wang H / Bueler SA / Rubinstein JL | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis of V-ATPase V region assembly by Vma12p, 21p, and 22p. Authors: Hanlin Wang / Stephanie A Bueler / John L Rubinstein / ![]() Abstract: Vacuolar-type adenosine triphosphatases (V-ATPases) are rotary proton pumps that acidify specific intracellular compartments in almost all eukaryotic cells. These multi-subunit enzymes consist of a ...Vacuolar-type adenosine triphosphatases (V-ATPases) are rotary proton pumps that acidify specific intracellular compartments in almost all eukaryotic cells. These multi-subunit enzymes consist of a soluble catalytic V region and a membrane-embedded proton-translocating V region. V is assembled in the endoplasmic reticulum (ER) membrane, and V is assembled in the cytosol. However, V binds V only after V is transported to the Golgi membrane, thereby preventing acidification of the ER. We isolated V complexes and subcomplexes from bound to V-ATPase assembly factors Vma12p, Vma21p, and Vma22p. Electron cryomicroscopy shows how the Vma12-22p complex recruits subunits a, e, and f to the rotor ring of V while blocking premature binding of V. Vma21p, which contains an ER-retrieval motif, binds the V:Vma12-22p complex, "mature" V, and a complex that appears to contain a ring of loosely packed rotor subunits and the proteins YAR027W and YAR028W. The structures suggest that Vma21p binds assembly intermediates that contain a rotor ring and that activation of proton pumping following assembly of V with V removes Vma21p, allowing V-ATPase to remain in the Golgi. Together, these structures show how Vma12-22p and Vma21p function in V-ATPase assembly and quality control, ensuring the enzyme acidifies only its intended cellular targets. #1: ![]() Title: Structural basis of V-ATPase V0 region assembly by Vma12p, 21p, and 22p Authors: Wang H / Bueler SA / Rubinstein JL | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 118 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 29.9 KB 29.9 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 10.6 KB | Display | ![]() |
Images | ![]() | 51.2 KB | ||
Others | ![]() ![]() | 116.2 MB 116.2 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8eavMC ![]() 8easC ![]() 8eatC ![]() 8eauC M: atomic model generated by this map C: citing same article ( |
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Links
EMDB pages | ![]() ![]() |
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Map
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Voxel size | X=Y=Z: 1.03 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_27987_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_27987_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
+Entire : YAR027W and YAR028W in complex with c subunits from yeast VO complex
+Supramolecule #1: YAR027W and YAR028W in complex with c subunits from yeast VO complex
+Macromolecule #1: YAR027W or YAR028W
+Macromolecule #2: YAR027W or YAR028W
+Macromolecule #3: YAR027W or YAR028W
+Macromolecule #4: YAR027W or YAR028W
+Macromolecule #5: subunit from the c ring of yeast VO complex
+Macromolecule #6: subunit from the c ring of yeast VO complex
+Macromolecule #7: YAR027W or YAR028W
+Macromolecule #8: YAR027W or YAR028W
+Macromolecule #9: YAR027W or YAR028W
+Macromolecule #10: YAR027W or YAR028W
+Macromolecule #11: YAR027W or YAR028W
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 |
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Grid | Model: Homemade / Material: COPPER/RHODIUM |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 80 % / Chamber temperature: 277 K |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 49.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.5 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |