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Yorodumi- EMDB-10380: Structure of rabbit 80S ribosome translating beta-tubulin in comp... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-10380 | ||||||||||||
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Title | Structure of rabbit 80S ribosome translating beta-tubulin in complex with tetratricopeptide protein 5 and nascent chain-associated complex | ||||||||||||
Map data | Structure of human TTC5 bound to the rabbit 80S ribosome translating beta-tubulin Sharpened, MTF-corrected map with the calibrated pixel size | ||||||||||||
Sample |
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Function / homology | Function and homology information positive regulation of mRNA catabolic process / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / cellular response to starvation / cytosolic ribosome / Regulation of TP53 Activity through Methylation / ribosome binding / 5S rRNA binding / cytosolic large ribosomal subunit / cytoplasmic vesicle / ribosome ...positive regulation of mRNA catabolic process / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / cellular response to starvation / cytosolic ribosome / Regulation of TP53 Activity through Methylation / ribosome binding / 5S rRNA binding / cytosolic large ribosomal subunit / cytoplasmic vesicle / ribosome / mitochondrial matrix / structural constituent of ribosome / ribonucleoprotein complex / translation / DNA repair / DNA damage response / chromatin binding / nucleolus / positive regulation of transcription by RNA polymerase II / mitochondrion / DNA binding / RNA binding / nucleoplasm / cytosol / cytoplasm Similarity search - Function | ||||||||||||
Biological species | Oryctolagus cuniculus (rabbit) / Homo sapiens (human) / Rabbit (rabbit) | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.11 Å | ||||||||||||
Authors | Lin Z / Gasic I / Chandrasekaran V / Peters N / Shao S / Ramakrishnan V / Mitchison TJ / Hegde RS | ||||||||||||
Funding support | United Kingdom, 3 items
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Citation | Journal: Science / Year: 2020 Title: TTC5 mediates autoregulation of tubulin via mRNA degradation. Authors: Zhewang Lin / Ivana Gasic / Viswanathan Chandrasekaran / Niklas Peters / Sichen Shao / Timothy J Mitchison / Ramanujan S Hegde / Abstract: Tubulins play crucial roles in cell division, intracellular traffic, and cell shape. Tubulin concentration is autoregulated by feedback control of messenger RNA (mRNA) degradation via an unknown ...Tubulins play crucial roles in cell division, intracellular traffic, and cell shape. Tubulin concentration is autoregulated by feedback control of messenger RNA (mRNA) degradation via an unknown mechanism. We identified tetratricopeptide protein 5 (TTC5) as a tubulin-specific ribosome-associating factor that triggers cotranslational degradation of tubulin mRNAs in response to excess soluble tubulin. Structural analysis revealed that TTC5 binds near the ribosome exit tunnel and engages the amino terminus of nascent tubulins. TTC5 mutants incapable of ribosome or nascent tubulin interaction abolished tubulin autoregulation and showed chromosome segregation defects during mitosis. Our findings show how a subset of mRNAs can be targeted for coordinated degradation by a specificity factor that recognizes the nascent polypeptides they encode. | ||||||||||||
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_10380.map.gz | 24.6 MB | EMDB map data format | |
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Header (meta data) | emd-10380-v30.xml emd-10380.xml | 75.9 KB 75.9 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_10380_fsc.xml | 14.1 KB | Display | FSC data file |
Images | emd_10380.png | 214.3 KB | ||
Masks | emd_10380_msk_1.map | 244.1 MB | Mask map | |
Others | emd_10380_additional.map.gz emd_10380_half_map_1.map.gz emd_10380_half_map_2.map.gz | 193.1 MB 194.4 MB 194.5 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-10380 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-10380 | HTTPS FTP |
-Related structure data
Related structure data | 6t59MC 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_10380.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Structure of human TTC5 bound to the rabbit 80S ribosome translating beta-tubulin Sharpened, MTF-corrected map with the calibrated pixel size | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.33 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
File | emd_10380_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Additional map: Unsharpened map Note that the pixel size has not been calibrated.
File | emd_10380_additional.map | ||||||||||||
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Annotation | Unsharpened map Note that the pixel size has not been calibrated. | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half1 map Note that the pixel size has not been calibrated.
File | emd_10380_half_map_1.map | ||||||||||||
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Annotation | Half1 map Note that the pixel size has not been calibrated. | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half2 map Note that the pixel size has not been calibrated.
File | emd_10380_half_map_2.map | ||||||||||||
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Annotation | Half2 map Note that the pixel size has not been calibrated. | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
+Entire : Rabbit 80S ribosome synthesizing beta-tubulin in complex with TTC5
+Supramolecule #1: Rabbit 80S ribosome synthesizing beta-tubulin in complex with TTC5
+Supramolecule #2: Ribosome
+Supramolecule #3: Tetratricopeptide repeat protein 5
+Macromolecule #1: Ribosomal protein L8
+Macromolecule #2: uL3
+Macromolecule #3: uL4
+Macromolecule #4: 60S ribosomal protein L5
+Macromolecule #5: 60S ribosomal protein L6
+Macromolecule #6: Ul30
+Macromolecule #7: eL8
+Macromolecule #8: uL6
+Macromolecule #9: 60S ribosomal protein L10
+Macromolecule #10: Ribosomal protein L11
+Macromolecule #11: eL13
+Macromolecule #12: Ribosomal protein L14
+Macromolecule #13: Ribosomal protein L15
+Macromolecule #14: uL13
+Macromolecule #15: uL22
+Macromolecule #16: eL18
+Macromolecule #17: eL19
+Macromolecule #18: eL20
+Macromolecule #19: eL21
+Macromolecule #20: eL22
+Macromolecule #21: Ribosomal protein L23
+Macromolecule #22: eL24
+Macromolecule #23: uL23
+Macromolecule #24: Ribosomal protein L26
+Macromolecule #25: 60S ribosomal protein L27
+Macromolecule #26: uL15
+Macromolecule #27: eL29
+Macromolecule #28: eL30
+Macromolecule #29: eL31
+Macromolecule #30: eL32
+Macromolecule #31: eL33
+Macromolecule #32: eL34
+Macromolecule #33: uL29
+Macromolecule #34: 60S ribosomal protein L36
+Macromolecule #35: Ribosomal protein L37
+Macromolecule #36: eL38
+Macromolecule #37: eL39
+Macromolecule #38: eL40
+Macromolecule #39: 60s ribosomal protein l41
+Macromolecule #40: eL42
+Macromolecule #41: eL43
+Macromolecule #42: eL28
+Macromolecule #43: uL10
+Macromolecule #44: Ribosomal protein L12
+Macromolecule #49: Nascent polypeptide-associated complex subunit alpha N-terminal region
+Macromolecule #50: Nascent polypeptide-associated complex subunit alpha
+Macromolecule #51: Transcription factor BTF3
+Macromolecule #52: Tetratricopeptide repeat protein 5
+Macromolecule #53: Tubulin Beta
+Macromolecule #45: P-site tRNA
+Macromolecule #46: 28S ribosomal RNA
+Macromolecule #47: 5S ribosomal RNA
+Macromolecule #48: 5.8S ribosomal RNA
+Macromolecule #54: MAGNESIUM ION
+Macromolecule #55: ZINC ION
-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 | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy |
Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: INTEGRATING / Average electron dose: 48.36 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |