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- PDB-9e6q: Cryo-EM structure of the Pyrobaculum calidifontis 50S ribosomal s... -
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Open data
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Basic information
Entry | Database: PDB / ID: 9e6q | ||||||
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Title | Cryo-EM structure of the Pyrobaculum calidifontis 50S ribosomal subunit in complex with Dri | ||||||
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![]() | RIBOSOME / Translation / Hibernation / RNA | ||||||
Function / homology | ![]() ribonuclease P activity / tRNA 5'-leader removal / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosome biogenesis / large ribosomal subunit / 5S rRNA binding / ribosomal large subunit assembly / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation ...ribonuclease P activity / tRNA 5'-leader removal / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosome biogenesis / large ribosomal subunit / 5S rRNA binding / ribosomal large subunit assembly / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / mRNA binding / RNA binding / zinc ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 1.95 Å | ||||||
![]() | Nissley, A.J. / Cate, J.H.D. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of an archaeal ribosome reveals a divergent active site and hibernation factor. Authors: Amos J Nissley / Yekaterina Shulgina / Roan W Kivimae / Blake E Downing / Petar I Penev / Jillian F Banfield / Dipti D Nayak / Jamie H D Cate / ![]() ![]() Abstract: Ribosomes translate mRNA into protein. Despite divergence in ribosome structure over the course of evolution, the catalytic site, known as the peptidyl transferase centre (PTC), is thought to be ...Ribosomes translate mRNA into protein. Despite divergence in ribosome structure over the course of evolution, the catalytic site, known as the peptidyl transferase centre (PTC), is thought to be nearly universally conserved. Here we identify clades of archaea that have highly divergent ribosomal RNA sequences in the PTC. To understand how these PTC sequences fold, we determined cryo-EM structures of the 70S and 50S ribosomes to 2.4 Å and 2 Å, respectively, from the hyperthermophilic archaeon Pyrobaculum calidifontis. PTC sequence variation leads to the rearrangement of key base triples, and differences between archaeal and bacterial ribosomal proteins enable sequence variation in archaeal PTCs. Finally, we identify an archaeal ribosome hibernation factor, Dri, that differs from known bacterial and eukaryotic hibernation factors and is found in multiple archaeal phyla. Overall, this work identifies factors that regulate ribosome function in archaea and reveals a larger diversity of the most ancient sequences in the ribosome. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 2.9 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.8 MB | Display | ![]() |
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Full document | ![]() | 2 MB | Display | |
Data in XML | ![]() | 204.8 KB | Display | |
Data in CIF | ![]() | 383.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 47578MC ![]() 9e71C ![]() 9e7fC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
-RNA chain , 2 types, 2 molecules 12
#1: RNA chain | Mass: 984007.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() |
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#2: RNA chain | Mass: 41803.953 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: GenBank: 126248349 |
-Protein , 7 types, 8 molecules 3AJAKAMAeAhAjAk
#3: Protein | Mass: 72127.695 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: A3MX58 | ||||||||||
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#13: Protein | Mass: 11470.542 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() ![]() #15: Protein | | Mass: 22623.768 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: A3MWR6 #33: Protein | | Mass: 7954.435 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: A3MTT1 #36: Protein | | Mass: 10603.610 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() #38: Protein | | Mass: 20956.449 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: A3MTM7 #39: Protein | | Mass: 10938.797 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: A3MWU0 |
+Large ribosomal subunit protein ... , 30 types, 30 molecules AAABACADAEAFAGAHAIALANAOAPAQARASATAUAVAWAXAYAZAaAbAcAdAfAgAi
-Non-polymers , 4 types, 8218 molecules 






#40: Chemical | ChemComp-SPM / #41: Chemical | ChemComp-MG / #42: Chemical | ChemComp-ZN / #43: Water | ChemComp-HOH / | |
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-Details
Has ligand of interest | N |
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Has protein modification | Y |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: 50S ribosomal subunit / Type: RIBOSOME / Entity ID: #1-#39 / Source: NATURAL | ||||||||||||||||||||||||||||||
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Molecular weight | Experimental value: NO | ||||||||||||||||||||||||||||||
Source (natural) | Organism: ![]() ![]() | ||||||||||||||||||||||||||||||
Buffer solution | pH: 7 | ||||||||||||||||||||||||||||||
Buffer component |
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Specimen | Conc.: 0.12 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||
Specimen support | Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: UltrAuFoil | ||||||||||||||||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 K |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: TFS KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 105000 X / Nominal defocus max: 1500 nm / Nominal defocus min: 500 nm |
Image recording | Electron dose: 40 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of grids imaged: 1 / Num. of real images: 7318 |
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Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||
Particle selection | Num. of particles selected: 2360632 | ||||||||||||
3D reconstruction | Resolution: 1.95 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 183467 / Symmetry type: POINT | ||||||||||||
Atomic model building | Protocol: AB INITIO MODEL |