[English] 日本語

- PDB-9i05: Cryo-EM structure of the large subunit of the mitochondrial ribos... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 9i05 | |||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Title | Cryo-EM structure of the large subunit of the mitochondrial ribosome from Toxoplasma gondii | |||||||||||||||||||||||||||
![]() |
| |||||||||||||||||||||||||||
![]() | RIBOSOME / Toxoplasma gondii / parasite / mitochondrial ribosome / LSU / large subunit | |||||||||||||||||||||||||||
Function / homology | ![]() regulation of mitochondrial mRNA stability / ribonucleoprotein granule / mitochondrial RNA processing / mitochondrial large ribosomal subunit / mitochondrial translation / cyclosporin A binding / RNA polymerase II CTD heptapeptide repeat P3 isomerase activity / RNA polymerase II CTD heptapeptide repeat P6 isomerase activity / peptidylprolyl isomerase / ubiquitin-protein transferase activity ...regulation of mitochondrial mRNA stability / ribonucleoprotein granule / mitochondrial RNA processing / mitochondrial large ribosomal subunit / mitochondrial translation / cyclosporin A binding / RNA polymerase II CTD heptapeptide repeat P3 isomerase activity / RNA polymerase II CTD heptapeptide repeat P6 isomerase activity / peptidylprolyl isomerase / ubiquitin-protein transferase activity / protein folding / large ribosomal subunit / transferase activity / 5S rRNA binding / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / mitochondrial matrix / translation / DNA-binding transcription factor activity / ribonucleoprotein complex / mRNA binding / DNA binding / RNA binding / nucleus / membrane / cytoplasm Similarity search - Function | |||||||||||||||||||||||||||
Biological species | ![]() ![]() | |||||||||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.2 Å | |||||||||||||||||||||||||||
![]() | Tobiasson, V. / Shikha, S. / Muhleip, A. | |||||||||||||||||||||||||||
Funding support | ![]()
| |||||||||||||||||||||||||||
![]() | ![]() Title: Numerous rRNA molecules form the apicomplexan mitoribosome via repurposed protein and RNA elements. Authors: Shikha Shikha / Victor Tobiasson / Mariana Ferreira Silva / Jana Ovciarikova / Dario Beraldi / Alexander Mühleip / Lilach Sheiner / ![]() ![]() ![]() Abstract: Mitochondrial ribosomes (mitoribosomes) are essential, and their function of synthesising mitochondrial proteins is universal. The core of almost all mitoribosomes is formed from a small number of ...Mitochondrial ribosomes (mitoribosomes) are essential, and their function of synthesising mitochondrial proteins is universal. The core of almost all mitoribosomes is formed from a small number of long and self-folding rRNA molecules. In contrast, the mitoribosome of the apicomplexan parasite Toxoplasma gondii assembles from over 50 extremely short rRNA molecules. Here, we use cryo-EM to discover the features that enable this unusual mitoribosome to perform its function. We reveal that poly-A tails added to rRNA molecules are integrated into the ribosome, and we demonstrate their essentiality for mitoribosome formation and for parasite survival. This is a distinct function for poly-A tails, which are otherwise known primarily as stabilisers of messenger RNAs. Furthermore, while ribosomes typically consist of unique rRNA sequences, here nine sequences are used twice, each copy integrated in a different mitoribosome domain, revealing one of the mechanisms enabling the extreme mitochondrial genome reduction characteristic to Apicomplexa and to a large group of related microbial eukaryotes. Finally, several transcription factor-like proteins are repurposed to compensate for reduced or lost critical ribosomal domains, including members of the ApiAP2 family thus far considered to be DNA-binding transcription factors. | |||||||||||||||||||||||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 7.7 MB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | ![]() 52551MC ![]() 9hqvC M: map data used to model this data C: citing same article ( |
---|---|
Similar structure data | Similarity search - Function & homology ![]() |
-
Links
-
Assembly
Deposited unit | ![]()
|
---|---|
1 |
|
-
Components
+Putative LSU ribosomal protein ... , 2 types, 2 molecules AaAh
+Large ribosomal subunit protein ... , 10 types, 10 molecules AbAcAnApAqAuABADAFXe
+Protein , 34 types, 34 molecules AdAlAoAsAvAxAyAzAAAEAGAHXaXbXcXfXgXkXmXoXpXqXsXtXxXyXAXBXCXD...
+Ribosomal protein ... , 4 types, 4 molecules AeAiACXH
+Putative ribosomal protein ... , 3 types, 3 molecules AfAmAt
+Putative 50S ribosomal protein ... , 4 types, 4 molecules AgAjAkAw
+Ribosomal l25 family ... , 2 types, 2 molecules ArUa
+RAP domain-containing ... , 7 types, 8 molecules AIXdXhXiXjXlXvXr
+AP2 domain transcription factor ... , 2 types, 2 molecules XnXz
+Transmembrane ... , 2 types, 2 molecules XwXI
+Protein/peptide , 5 types, 5 molecules UbUcUdUeUf
+RNA chain , 32 types, 32 molecules RARBRCRDRERFRGRIRJRKRLRMRNRORPRQRSRTRURVRWRXRYRZRaRbRcRdRfRgRhRi
+Non-polymers , 2 types, 3 molecules 


+Details
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
---|---|
EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-
Sample preparation
Component | Name: mitochondrial ribososome from Toxoplasma gondii / Type: RIBOSOME / Entity ID: #1-#106 / Source: NATURAL |
---|---|
Molecular weight | Experimental value: NO |
Source (natural) | Organism: ![]() ![]() |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid type: Quantifoil R2/1 |
Vitrification | Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K |
-
Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
---|---|
Microscopy | Model: TFS KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1600 nm / Nominal defocus min: 600 nm |
Image recording | Electron dose: 35 e/Å2 / Film or detector model: GATAN K3 BIOCONTINUUM (6k x 4k) |
-
Processing
EM software | Name: PHENIX / Version: 1.21rc1_5058: / Category: model refinement | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 2.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 375745 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
|