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- PDB-8a98: CRYO-EM STRUCTURE OF LEISHMANIA MAJOR 80S RIBOSOME : snoRNA MUTANT -
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Open data
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Basic information
Entry | Database: PDB / ID: 8a98 | ||||||
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Title | CRYO-EM STRUCTURE OF LEISHMANIA MAJOR 80S RIBOSOME : snoRNA MUTANT | ||||||
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![]() | RIBOSOME / CRYO-EM / LEISHMANIA MAJOR / 80S RIBOSOME snoRNA MUTANT | ||||||
Function / homology | ![]() ciliary transition zone / ciliary plasm / nuclear lumen / negative regulation of translational frameshifting / endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / protein-RNA complex assembly / endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of LSU-rRNA / translation regulator activity / rescue of stalled ribosome ...ciliary transition zone / ciliary plasm / nuclear lumen / negative regulation of translational frameshifting / endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / protein-RNA complex assembly / endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of LSU-rRNA / translation regulator activity / rescue of stalled ribosome / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosomal large subunit biogenesis / protein kinase C binding / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / small-subunit processome / maintenance of translational fidelity / rRNA processing / kinase activity / ribosome biogenesis / ribosome binding / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / ribosomal large subunit assembly / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / small ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / mRNA binding / nucleolus / RNA binding / zinc ion binding / nucleoplasm / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.46 Å | ||||||
![]() | Rajan, K.S. / Yonath, A. / Bashan, A. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structural and mechanistic insights into the function of Leishmania ribosome lacking a single pseudouridine modification. Authors: K Shanmugha Rajan / Saurav Aryal / Disha-Gajanan Hiregange / Anat Bashan / Hava Madmoni / Mika Olami / Tirza Doniger / Smadar Cohen-Chalamish / Pascal Pescher / Masato Taoka / Yuko Nobe / ...Authors: K Shanmugha Rajan / Saurav Aryal / Disha-Gajanan Hiregange / Anat Bashan / Hava Madmoni / Mika Olami / Tirza Doniger / Smadar Cohen-Chalamish / Pascal Pescher / Masato Taoka / Yuko Nobe / Aliza Fedorenko / Tanaya Bose / Ella Zimermann / Eric Prina / Noa Aharon-Hefetz / Yitzhak Pilpel / Toshiaki Isobe / Ron Unger / Gerald F Späth / Ada Yonath / Shulamit Michaeli / ![]() ![]() ![]() Abstract: Leishmania is the causative agent of cutaneous and visceral diseases affecting millions of individuals worldwide. Pseudouridine (Ψ), the most abundant modification on rRNA, changes during the ...Leishmania is the causative agent of cutaneous and visceral diseases affecting millions of individuals worldwide. Pseudouridine (Ψ), the most abundant modification on rRNA, changes during the parasite life cycle. Alterations in the level of a specific Ψ in helix 69 (H69) affected ribosome function. To decipher the molecular mechanism of this phenotype, we determine the structure of ribosomes lacking the single Ψ and its parental strain at ∼2.4-3 Å resolution using cryo-EM. Our findings demonstrate the significance of a single Ψ on H69 to its structure and the importance for its interactions with helix 44 and specific tRNAs. Our study suggests that rRNA modification affects translation of mRNAs carrying codon bias due to selective accommodation of tRNAs by the ribosome. Based on the high-resolution structures, we propose a mechanism explaining how the ribosome selects specific tRNAs. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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-Validation report
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-Related structure data
Related structure data | ![]() 15272MC ![]() 8ovjC ![]() 8rxhC ![]() 8rxxC 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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Assembly
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Components
-Putative 40S ribosomal protein ... , 15 types, 15 molecules SWSYSVSUSTSRSCSDScSPSNSdSLSJK
#1: Protein | Mass: 17472.395 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4QBV0 |
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#3: Protein | Mass: 17035.592 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4QH01 |
#5: Protein | Mass: 16551.529 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4Q806 |
#6: Protein | Mass: 20023.457 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() |
#7: Protein | Mass: 17482.764 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4Q3M1 |
#9: Protein | Mass: 17433.422 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4Q1Y3 |
#11: Protein | Mass: 24511.762 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: BPK282A1 / References: UniProt: Q4Q4A0 |
#12: Protein | Mass: 22188.902 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4QIM3 |
#18: Protein | Mass: 9819.463 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: BPK282A1 / References: UniProt: Q4Q140 |
#22: Protein | Mass: 15969.643 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: BPK282A1 / References: UniProt: Q4QC89 |
#24: Protein | Mass: 18681.125 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4Q1X7 |
#25: Protein | Mass: 9763.191 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4Q931 |
#27: Protein | Mass: 16718.586 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: BPK282A1 / References: UniProt: Q4Q9A5 |
#28: Protein | Mass: 14719.258 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4QGW3 |
#61: Protein | Mass: 19948.615 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4QBJ1 |
-40S ribosomal protein ... , 15 types, 15 molecules SZSXSBSESKSaSeSQSOSISHSGSFSASb
#2: Protein | Mass: 15808.882 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4Q1D2 |
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#4: Protein | Mass: 18144.053 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: E9AEE8 |
#10: Protein | Mass: 27536.629 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4Q0Q0 |
#13: Protein | Mass: 30742.084 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4QG31 |
#14: Protein | Mass: 24984.250 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P25204 |
#17: Protein | Mass: 13071.399 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4Q9X4 |
#19: Protein | Mass: 7394.894 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4Q7P0 |
#21: Protein | Mass: 15627.837 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4QG97 |
#23: Protein | Mass: 15623.180 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4Q8H1 |
#29: Protein | Mass: 23765.207 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: E9AC32 |
#30: Protein | Mass: 21336.623 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q868B1 |
#31: Protein | Mass: 28370.227 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q9NE83 |
#32: Protein | Mass: 28791.135 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4QDL5 |
#33: Protein | Mass: 30062.037 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4FX73 |
#34: Protein | Mass: 12794.251 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4Q8L6 |
-Putative ribosomal protein ... , 7 types, 7 molecules SSSMBgXkC
#8: Protein | Mass: 6696.929 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4Q817 |
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#26: Protein | Mass: 13031.983 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: BPK282A1 / References: UniProt: Q4Q8G4 |
#45: Protein | Mass: 47593.660 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4Q2Q6 |
#68: Protein | Mass: 16492.312 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4QHL3 |
#76: Protein | Mass: 14608.168 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4Q1W6 |
#77: Protein | Mass: 9479.287 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: BPK282A1 / References: UniProt: Q4Q8X0 |
#80: Protein | Mass: 41096.855 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: E9ADW5 |
-RNA chain , 10 types, 10 molecules S4S112478563
#15: RNA chain | Mass: 6106.721 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() |
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#20: RNA chain | Mass: 710459.375 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() |
#41: RNA chain | Mass: 577004.438 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() |
#42: RNA chain | Mass: 492524.812 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() |
#43: RNA chain | Mass: 59144.129 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: GenBank: 321438308 |
#44: RNA chain | Mass: 54952.504 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: GenBank: 1207899567 |
#46: RNA chain | Mass: 39451.383 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() |
#47: RNA chain | Mass: 43481.770 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: GenBank: 321438308 |
#58: RNA chain | Mass: 23336.938 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: GenBank: 321438308 |
#81: RNA chain | Mass: 69146.633 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: GenBank: 321438308 |
-Protein , 3 types, 3 molecules SgShI
#16: Protein | Mass: 34441.516 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4Q7Y7 |
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#35: Protein | Mass: 25229.275 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4Q5K7 |
#53: Protein | Mass: 24805.891 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: E9AEA8 |
-60S ribosomal protein ... , 10 types, 10 molecules fdbGPRDYon
#36: Protein | Mass: 15458.153 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4QC11 |
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#37: Protein | Mass: 11370.224 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: E9AEK1 |
#40: Protein | Mass: 8001.308 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: MHOM/GT/2001/U1103 / References: UniProt: Q4Q178 |
#50: Protein | Mass: 29824.182 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4QIP1 |
#54: Protein | Mass: 22071.080 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4QG98 |
#56: Protein | Mass: 20852.338 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4Q5J4 |
#62: Protein | Mass: 21694.502 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P48157 |
#64: Protein | Mass: 15469.330 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4Q504 |
#75: Protein | Mass: 10337.223 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4QC01 |
#79: Protein/peptide | Mass: 4390.496 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() |
+Putative 60S ... , 21 types, 21 molecules caAOHQETSLZFhJVWUiple
-Ribosomal protein ... , 2 types, 2 molecules Mj
#52: Protein | Mass: 24497.971 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q4Q6S3 |
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#83: Protein | Mass: 9862.590 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: E9AEH2 |
-Non-polymers , 5 types, 2431 molecules 








#84: Chemical | ChemComp-MG / #85: Chemical | ChemComp-ZN / #86: Chemical | ChemComp-NA / #87: Chemical | #88: Water | ChemComp-HOH / | |
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-Details
Has ligand of interest | Y |
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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: CRYO-EM STRUCTURE OF LEISHMANIA MAJOR 80S RIBOSOME snoRNA MUTANT Type: RIBOSOME Details: CRYO-EM STRUCTURE OF LEISHMANIA MAJOR 80S RIBOSOME snoRNA MUTANT Entity ID: #1-#83 / Source: NATURAL | ||||||||||||||||||||||||
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Source (natural) | Organism: ![]() | ||||||||||||||||||||||||
Buffer solution | pH: 7.6 | ||||||||||||||||||||||||
Buffer component |
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Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
Specimen support | Grid material: COPPER / Grid type: Quantifoil R2/2 | ||||||||||||||||||||||||
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: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1500 nm / Nominal defocus min: 500 nm |
Image recording | Electron dose: 1 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
Software | Name: PHENIX / Version: (1.20.1_4487:phenix.real_space_refine) / Classification: refinement | ||||||||||||||||||||||||||||
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EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||
3D reconstruction | Resolution: 2.46 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 345376 / Symmetry type: POINT | ||||||||||||||||||||||||||||
Atomic model building |
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Refinement | Cross valid method: THROUGHOUT | ||||||||||||||||||||||||||||
Displacement parameters | Biso max: 271.93 Å2 / Biso mean: 50.2839 Å2 / Biso min: 0 Å2 |