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Yorodumi- EMDB-54489: Tomogram of a yeast cell treated with alpha-factor (bud region) -
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Open data
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Basic information
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| Title | Tomogram of a yeast cell treated with alpha-factor (bud region) | |||||||||
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Keywords | myosin-adaptor / lipid droplet motility / CYTOSOLIC PROTEIN | |||||||||
| Biological species | ![]() | |||||||||
| Method | electron tomography / cryo EM | |||||||||
Authors | Keller J / Diep DTV / Zhao X-T / Bohnert M / Fernandez-Busnadiego R | |||||||||
| Funding support | Germany, 1 items
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Citation | Journal: Cell Rep / Year: 2025Title: The Myo2 adaptor Ldm1 and its receptor Ldo16 mediate actin-dependent lipid droplet motility. Authors: Xue-Tong Zhao / Duy Trong Vien Diep / Louis Percifull / Rebecca Martina Fausten / Marie Hugenroth / Pascal Höhne / Beatriz Leite / Bianca Marie Esch / Javier Collado / Jenny Keller / ...Authors: Xue-Tong Zhao / Duy Trong Vien Diep / Louis Percifull / Rebecca Martina Fausten / Marie Hugenroth / Pascal Höhne / Beatriz Leite / Bianca Marie Esch / Javier Collado / Jenny Keller / Stephan Wilmes / Meryem Aysenur Turhan / Mike Wälte / Thomas Becker / Daniel Kümmel / Christian Schuberth / Rubén Fernández-Busnadiego / Florian Fröhlich / Roland Wedlich-Söldner / Maria Bohnert / ![]() Abstract: Organelle motility enables strategic cellular reorganizations. In yeast, this process depends on the actin cytoskeleton, type V myosin motor proteins, and organelle-specific myosin adaptor proteins. ...Organelle motility enables strategic cellular reorganizations. In yeast, this process depends on the actin cytoskeleton, type V myosin motor proteins, and organelle-specific myosin adaptor proteins. While the myosin adaptors for most organelles are known, the coupling of myosin to lipid droplets (LDs), the cellular lipid storage organelles, remained enigmatic. Using genome-wide screening, we identified Ldm1 (lipid droplet motility 1/Yer085c) as a myosin adaptor. Ldm1 binds to the globular tail domain of the myosin Myo2 and to the LD surface protein Ldo16 to enable actin-dependent LD motility. Ldo16 has additional roles in LD contact sites to the vacuole and the endoplasmic reticulum, suggesting a coordination of LD motility and organelle tethering. Ldm1 has a second role in mitochondrial transport, and elevated Ldm1 levels rescue defects of the mitochondrial Myo2-adaptors Mmr1/Ypt11. Our work identifies the molecular machinery for LD motility and contributes to a comprehensive understanding of acto-myosin-based cellular reorganization. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_54489.map.gz | 1.2 GB | EMDB map data format | |
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| Header (meta data) | emd-54489-v30.xml emd-54489.xml | 10.6 KB 10.6 KB | Display Display | EMDB header |
| Images | emd_54489.png | 257.4 KB | ||
| Filedesc metadata | emd-54489.cif.gz | 3.8 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-54489 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-54489 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_54489.map.gz / Format: CCP4 / Size: 1.3 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. generated in cubic-lattice coordinate | ||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 14.6 Å | ||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : Tomogram of yeast cell overexpressing Ldm1, treated with alpha-fa...
| Entire | Name: Tomogram of yeast cell overexpressing Ldm1, treated with alpha-factor (unbudded region) |
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| Components |
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-Supramolecule #1: Tomogram of yeast cell overexpressing Ldm1, treated with alpha-fa...
| Supramolecule | Name: Tomogram of yeast cell overexpressing Ldm1, treated with alpha-factor (unbudded region) type: cell / ID: 1 / Parent: 0 / Details: from FIB-milled yeast lamella |
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| Source (natural) | Organism: ![]() |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | electron tomography |
| Aggregation state | cell |
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Sample preparation
| Buffer | pH: 7.5 |
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| Vitrification | Cryogen name: ETHANE-PROPANE |
| Sectioning | Focused ion beam - Instrument: OTHER / Focused ion beam - Ion: OTHER / Focused ion beam - Voltage: 30 / Focused ion beam - Current: 0.05 / Focused ion beam - Duration: 3600 / Focused ion beam - Temperature: 83 K / Focused ion beam - Initial thickness: 5000 / Focused ion beam - Final thickness: 120 Focused ion beam - Details: The value given for _em_focused_ion_beam.instrument is Aquilos 2. This is not in a list of allowed values {'DB235', 'OTHER'} so OTHER is written into the XML file. |
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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) / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Average electron dose: 3.29 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 50.0 µm / Calibrated defocus max: 7.0 µm / Calibrated defocus min: 5.0 µm / Calibrated magnification: 33000 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 7.0 µm / Nominal defocus min: 5.0 µm / Nominal magnification: 33000 |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
| Final reconstruction | Software - Name: IMOD (ver. 4.12) / Number images used: 37 |
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| CTF correction | Type: NONE |
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Keywords
Authors
Germany, 1 items
Citation


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FIELD EMISSION GUN
