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Yorodumi- PDB-8oo0: Chaetomium thermophilum Methionine Aminopeptidase 2 autoproteolys... -
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-Basic information
Entry | Database: PDB / ID: 8oo0 | ||||||
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Title | Chaetomium thermophilum Methionine Aminopeptidase 2 autoproteolysis product at the 80S ribosome | ||||||
Components |
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Keywords | METAL BINDING PROTEIN / Ribosome Associated Factor / Protease / A-site / Factor binding site / Decoding center / Protein Maturation / Proteostasis / NME / p67 / p26 / Autoproteolysis / MAP / MetAP / MAP2 / MetAP2 | ||||||
Function / homology | Function and homology information dolichyl-diphosphooligosaccharide-protein glycotransferase / dolichyl-diphosphooligosaccharide-protein glycotransferase activity / initiator methionyl aminopeptidase activity / methionyl aminopeptidase / non-chaperonin molecular chaperone ATPase / metalloaminopeptidase activity / protein glycosylation / translation regulator activity / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / cytosolic ribosome ...dolichyl-diphosphooligosaccharide-protein glycotransferase / dolichyl-diphosphooligosaccharide-protein glycotransferase activity / initiator methionyl aminopeptidase activity / methionyl aminopeptidase / non-chaperonin molecular chaperone ATPase / metalloaminopeptidase activity / protein glycosylation / translation regulator activity / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / cytosolic ribosome / methyltransferase activity / ATP-dependent protein folding chaperone / ribosomal small subunit assembly / cytosolic small ribosomal subunit / ribosome binding / large ribosomal subunit / ribosome biogenesis / cytoplasmic translation / small ribosomal subunit / methylation / 5S rRNA binding / cytosolic large ribosomal subunit / rRNA binding / ribosome / structural constituent of ribosome / ribonucleoprotein complex / translation / ATP hydrolysis activity / proteolysis / RNA binding / zinc ion binding / ATP binding / membrane / metal ion binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Thermochaetoides thermophila DSM 1495 (fungus) Thermochaetoides thermophila (fungus) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å | ||||||
Authors | Klein, M.A. / Wild, K. / Kisonaite, M. / Sinning, I. | ||||||
Funding support | Germany, 1items
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Citation | Journal: Nat Commun / Year: 2024 Title: Methionine aminopeptidase 2 and its autoproteolysis product have different binding sites on the ribosome. Authors: Marius A Klein / Klemens Wild / Miglė Kišonaitė / Irmgard Sinning / Abstract: Excision of the initiator methionine is among the first co-translational processes that occur at the ribosome. While this crucial step in protein maturation is executed by two types of methionine ...Excision of the initiator methionine is among the first co-translational processes that occur at the ribosome. While this crucial step in protein maturation is executed by two types of methionine aminopeptidases in eukaryotes (MAP1 and MAP2), additional roles in disease and translational regulation have drawn more attention to MAP2. Here, we report several cryo-EM structures of human and fungal MAP2 at the 80S ribosome. Irrespective of nascent chains, MAP2 can occupy the tunnel exit. On nascent chain displaying ribosomes, the MAP2-80S interaction is highly dynamic and the MAP2-specific N-terminal extension engages in stabilizing interactions with the long rRNA expansion segment ES27L. Loss of this extension by autoproteolytic cleavage impedes interactions at the tunnel, while promoting MAP2 to enter the ribosomal A-site, where it engages with crucial functional centers of translation. These findings reveal that proteolytic remodeling of MAP2 severely affects ribosome binding, and set the stage for targeted functional studies. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8oo0.cif.gz | 4.6 MB | Display | PDBx/mmCIF format |
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PDB format | pdb8oo0.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 8oo0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oo/8oo0 ftp://data.pdbj.org/pub/pdb/validation_reports/oo/8oo0 | HTTPS FTP |
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-Related structure data
Related structure data | 17004MC 8onxC 8onyC 8onzC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-RNA chain , 4 types, 4 molecules 1234
#1: RNA chain | Mass: 1078730.125 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: GenBank: 7OLC_1 |
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#2: RNA chain | Mass: 578887.625 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermochaetoides thermophila DSM 1495 (fungus) Production host: Thermochaetoides thermophila DSM 1495 (fungus) References: GenBank: 7OLC_2 |
#3: RNA chain | Mass: 38596.891 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermochaetoides thermophila DSM 1495 (fungus) Production host: Thermochaetoides thermophila DSM 1495 (fungus) References: GenBank: 7OLC_3 |
#4: RNA chain | Mass: 50147.688 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermochaetoides thermophila DSM 1495 (fungus) Production host: Thermochaetoides thermophila (fungus) / References: GenBank: MT316345.1 |
-Protein , 7 types, 7 molecules ABCLhLmLsD
#5: Protein | Mass: 35149.641 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0S9U0 |
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#6: Protein | Mass: 32667.918 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0S428 |
#7: Protein | Mass: 67110.992 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) References: UniProt: G0SCU5, non-chaperonin molecular chaperone ATPase |
#41: Protein | Mass: 14643.441 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) References: UniProt: G0S0D7, dolichyl-diphosphooligosaccharide-protein glycotransferase |
#46: Protein | Mass: 14609.222 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: A0A2A9PNA8 |
#51: Protein | Mass: 33853.590 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0SGP3 |
#84: Protein | Mass: 41310.402 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermochaetoides thermophila (fungus) / Gene: CTHT_0063100 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: G0SEA9 |
+60S ribosomal protein ... , 32 types, 33 molecules LALBLCLDLELFLGLHLILKLLLMLOLPLSLTLULVLWLXLYLZLbLcLeLfLiLkLlLn...
-Putative ribosomal ... , 2 types, 2 molecules LJSS
#17: Protein | Mass: 20119.275 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0SHQ2 |
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#70: Protein | Mass: 17826.707 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0S6J7 |
-Ribosomal protein ... , 7 types, 7 molecules LNLQLRLaLgLjSb
#21: Protein | Mass: 24307.287 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0RZ88 |
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#24: Protein | Mass: 24195.535 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0S9B5 |
#25: Protein | Mass: 22409.201 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0S9T3 |
#34: Protein | Mass: 16848.539 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G2QB77 |
#40: Protein | Mass: 13492.993 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0SFN0 |
#43: Protein | Mass: 10660.455 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0S101 |
#79: Protein | Mass: 8923.572 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0S1S4 |
-Putative 60S ribosomal ... , 2 types, 2 molecules LdLq
#37: Protein | Mass: 13872.177 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0SD68 |
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#50: Protein | Mass: 15960.451 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0SHJ6 |
+40S ribosomal protein ... , 30 types, 30 molecules SASBSCSDSESFSGSHSISJSKSLSMSNSOSPSQSRSTSUSVSWSXSYSZSaScSdSeSf
-Non-polymers , 1 types, 8 molecules
#85: Chemical | ChemComp-ZN / |
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-Details
Has ligand of interest | N |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: MAP2 autoproteolysis product in complex with the 80S ribosome Type: COMPLEX / Entity ID: #1-#84 / Source: RECOMBINANT |
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Source (natural) | Organism: Thermochaetoides thermophila (fungus) |
Source (recombinant) | Organism: Spodoptera frugiperda (fall armyworm) |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-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: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2100 nm / Nominal defocus min: 1100 nm |
Image recording | Electron dose: 54.8 e/Å2 / Film or detector model: GATAN K2 QUANTUM (4k x 4k) |
-Processing
EM software | Name: PHENIX / Version: 1.19_4092 / Category: model refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 119160 / Symmetry type: POINT | ||||||||||||||||||||||||
Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||
Displacement parameters | Biso mean: 108.07 Å2 | ||||||||||||||||||||||||
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