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Open data
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Basic information
| Entry | Database: PDB / ID: 8p2k | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Title | Ternary complex of translating ribosome, NAC and METAP1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Keywords | TRANSLATION / ribosome / methionine aminopeptidase 1 / methionine excision / protein biogenesis / nascent chain | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationnegative regulation of striated muscle cell apoptotic process / Isomerases; Racemases and epimerases; Acting on carbohydrates and derivatives / regulation of skeletal muscle fiber development / positive regulation of cell proliferation involved in heart morphogenesis / positive regulation of skeletal muscle tissue growth / racemase and epimerase activity, acting on carbohydrates and derivatives / glucose-6-phosphate isomerase / negative regulation of protein localization to endoplasmic reticulum / nascent polypeptide-associated complex / glucose-6-phosphate isomerase activity ...negative regulation of striated muscle cell apoptotic process / Isomerases; Racemases and epimerases; Acting on carbohydrates and derivatives / regulation of skeletal muscle fiber development / positive regulation of cell proliferation involved in heart morphogenesis / positive regulation of skeletal muscle tissue growth / racemase and epimerase activity, acting on carbohydrates and derivatives / glucose-6-phosphate isomerase / negative regulation of protein localization to endoplasmic reticulum / nascent polypeptide-associated complex / glucose-6-phosphate isomerase activity / cardiac ventricle development / hemostasis / glucose 6-phosphate metabolic process / methionyl aminopeptidase / initiator methionyl aminopeptidase activity / heart trabecula morphogenesis / carbohydrate derivative binding / metalloexopeptidase activity / skeletal muscle tissue regeneration / fructose 6-phosphate metabolic process / monosaccharide binding / Gluconeogenesis / Glycolysis / canonical glycolysis / ciliary membrane / positive regulation of immunoglobulin production / response to testosterone / erythrocyte homeostasis / negative regulation of glycolytic process through fructose-6-phosphate / organelle membrane / metalloaminopeptidase activity / response to immobilization stress / laminin receptor activity / humoral immune response / mesoderm formation / Peptide chain elongation / Selenocysteine synthesis / aminopeptidase activity / Formation of a pool of free 40S subunits / response to cadmium ion / Eukaryotic Translation Termination / SRP-dependent cotranslational protein targeting to membrane / Response of EIF2AK4 (GCN2) to amino acid deficiency / ubiquitin ligase inhibitor activity / 90S preribosome / Viral mRNA Translation / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / positive regulation of signal transduction by p53 class mediator / GTP hydrolysis and joining of the 60S ribosomal subunit / L13a-mediated translational silencing of Ceruloplasmin expression / Major pathway of rRNA processing in the nucleolus and cytosol / phagocytic cup / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / maturation of LSU-rRNA / protein-RNA complex assembly / response to muscle stretch / translation regulator activity / response to progesterone / rough endoplasmic reticulum / ribosomal small subunit export from nucleus / laminin binding / gastrulation / positive regulation of endothelial cell migration / MDM2/MDM4 family protein binding / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / cytokine activity / cytosolic ribosome / DNA-(apurinic or apyrimidinic site) lyase / glycolytic process / gluconeogenesis / ribosomal large subunit biogenesis / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / TP53 Regulates Metabolic Genes / growth factor activity / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / positive regulation of apoptotic signaling pathway / wound healing / maturation of SSU-rRNA / protein maturation / small-subunit processome / platelet aggregation / spindle / Regulation of expression of SLITs and ROBOs / cytoplasmic ribonucleoprotein granule / rRNA processing / response to estradiol / rhythmic process / positive regulation of canonical Wnt signaling pathway / regulation of translation / antimicrobial humoral immune response mediated by antimicrobial peptide / heparin binding / protein transport / glucose homeostasis / large ribosomal subunit / Inactivation, recovery and regulation of the phototransduction cascade / ribosomal small subunit assembly / virus receptor activity / ribosome binding / ribosomal small subunit biogenesis / 5S rRNA binding Similarity search - Function | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Biological species | ![]() Homo sapiens (human) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Authors | Jia, M. / Jaskolowski, M. / Scaiola, A. / Jomaa, A. / Ban, N. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Funding support | Switzerland, Germany, 4items
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Citation | Journal: Science / Year: 2023Title: NAC controls cotranslational N-terminal methionine excision in eukaryotes. Authors: Martin Gamerdinger / Min Jia / Renate Schloemer / Laurenz Rabl / Mateusz Jaskolowski / Katrin M Khakzar / Zeynel Ulusoy / Annalena Wallisch / Ahmad Jomaa / Gundula Hunaeus / Alain Scaiola / ...Authors: Martin Gamerdinger / Min Jia / Renate Schloemer / Laurenz Rabl / Mateusz Jaskolowski / Katrin M Khakzar / Zeynel Ulusoy / Annalena Wallisch / Ahmad Jomaa / Gundula Hunaeus / Alain Scaiola / Kay Diederichs / Nenad Ban / Elke Deuerling / ![]() Abstract: N-terminal methionine excision from newly synthesized proteins, catalyzed cotranslationally by methionine aminopeptidases (METAPs), is an essential and universally conserved process that plays a key ...N-terminal methionine excision from newly synthesized proteins, catalyzed cotranslationally by methionine aminopeptidases (METAPs), is an essential and universally conserved process that plays a key role in cell homeostasis and protein biogenesis. However, how METAPs interact with ribosomes and how their cleavage specificity is ensured is unknown. We discovered that in eukaryotes the nascent polypeptide-associated complex (NAC) controls ribosome binding of METAP1. NAC recruits METAP1 using a long, flexible tail and provides a platform for the formation of an active methionine excision complex at the ribosomal tunnel exit. This mode of interaction ensures the efficient excision of methionine from cytosolic proteins, whereas proteins targeted to the endoplasmic reticulum are spared. Our results suggest a broader mechanism for how access of protein biogenesis factors to translating ribosomes is controlled. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8p2k.cif.gz | 7.1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8p2k.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 8p2k.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/p2/8p2k ftp://data.pdbj.org/pub/pdb/validation_reports/p2/8p2k | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 17367MC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-RNA chain , 6 types, 6 molecules B5B7B8A2AIAT
| #1: RNA chain | Mass: 1557519.500 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #2: RNA chain | Mass: 38691.914 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #3: RNA chain | Mass: 50809.047 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #52: RNA chain | Mass: 603928.250 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #60: RNA chain | Mass: 15209.544 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #61: RNA chain | Mass: 24451.561 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+60S ribosomal protein ... , 28 types, 28 molecules BABCBEBGBHBIBJBLBMBOBSBTBUBZBaBbBcBdBfBgBhBiBkBlBpBrBtAz
-Ribosomal protein ... , 14 types, 14 molecules BBBDBFBNBRBVBWBYBeBjBvACAeAv
| #5: Protein | Mass: 46120.996 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #7: Protein | Mass: 34509.879 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #9: Protein | Mass: 29201.836 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #17: Protein | Mass: 24207.285 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #21: Protein | Mass: 23535.281 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #25: Protein | Mass: 14892.505 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #26: Protein | Mass: 17825.111 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #28: Protein | Mass: 17303.363 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #34: Protein | Mass: 15898.932 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #39: Protein | Mass: 11111.032 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #48: Protein | Mass: 24875.410 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #55: Protein | Mass: 18004.041 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #67: Protein | Mass: 22913.453 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #84: Protein | Mass: 14865.555 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein , 14 types, 14 molecules BKBPBQBXBmBoBsMANaNbAEAFAjAp
| #14: Protein | Mass: 7967.228 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #19: Protein | Mass: 21444.221 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #20: Protein | Mass: 21699.688 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #27: Protein | Mass: 17768.246 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #42: Protein | Mass: 14800.474 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #43: Protein | Mass: 12489.991 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #46: Protein | Mass: 34380.504 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #49: Protein | Mass: 43274.195 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: METAP1, KIAA0094 / Production host: ![]() |
| #50: Protein | Mass: 23406.824 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NACA, HSD48 / Production host: ![]() |
| #51: Protein | Mass: 14493.821 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: BTF3 / Production host: ![]() |
| #57: Protein | Mass: 13047.532 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #58: Protein | Mass: 35115.652 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #72: Protein | Mass: 18933.846 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #78: Protein | Mass: 19213.465 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+40S ribosomal protein ... , 26 types, 26 molecules AAABADAGAZAaAbAcAdAfAgAhAiAkAlAmAnAoAqArAsAtAuAwAxAy
-Non-polymers , 9 types, 2965 molecules 
















| #89: Chemical | ChemComp-N / #90: Chemical | ChemComp-SPD / #91: Chemical | #92: Chemical | ChemComp-MG / #93: Chemical | ChemComp-UNX / #94: Chemical | ChemComp-GTP / | #95: Chemical | ChemComp-AAC / | #96: Chemical | ChemComp-ZN / #97: 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
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| Buffer solution | pH: 7.6 | ||||||||||||||||||||||||
| 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-PROPANE / 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: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 81000 X / Nominal defocus max: 2400 nm / Nominal defocus min: 600 nm |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 21221 / Algorithm: FOURIER SPACE / Symmetry type: POINT | ||||||||||||||||||||||||||||
| Atomic model building | Protocol: RIGID BODY FIT / Space: REAL | ||||||||||||||||||||||||||||
| Atomic model building |
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| Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 115.48 Å2 | ||||||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi





Homo sapiens (human)
Switzerland,
Germany, 4items
Citation






PDBj













































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