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Open data
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Basic information
| Entry | Database: PDB / ID: 9s3d | ||||||||||||||||||||||||||||||
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| Title | NAC bound human RNC with 58 amino acid ARF1-linker | ||||||||||||||||||||||||||||||
Components |
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Keywords | RIBOSOME / co-translational / N-terminal myristoylation / myristoylation / NAC / ARF1 / NMT1 | ||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationnegative regulation of striated muscle cell apoptotic process / regulation of skeletal muscle fiber development / positive regulation of cell proliferation involved in heart morphogenesis / positive regulation of skeletal muscle tissue growth / translation termination factor activity / translation release factor complex / cardiac ventricle development / negative regulation of protein localization to endoplasmic reticulum / nascent polypeptide-associated complex / cytoplasmic translational termination ...negative regulation of striated muscle cell apoptotic process / regulation of skeletal muscle fiber development / positive regulation of cell proliferation involved in heart morphogenesis / positive regulation of skeletal muscle tissue growth / translation termination factor activity / translation release factor complex / cardiac ventricle development / negative regulation of protein localization to endoplasmic reticulum / nascent polypeptide-associated complex / cytoplasmic translational termination / heart trabecula morphogenesis / regulation of translational termination / translation release factor activity / skeletal muscle tissue regeneration / translation release factor activity, codon specific / male meiosis I / translation at presynapse / response to insecticide / sequence-specific mRNA binding / regulation of translation involved in cellular response to UV / eukaryotic 80S initiation complex / ribosomal protein import into nucleus / negative regulation of endoplasmic reticulum unfolded protein response / regulation of G1 to G0 transition / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / oxidized pyrimidine DNA binding / response to TNF agonist / positive regulation of base-excision repair / peptidyl-tRNA hydrolase activity / protein-DNA complex disassembly / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage / positive regulation of respiratory burst involved in inflammatory response / positive regulation of gastrulation / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway / protein methylation / protein tyrosine kinase inhibitor activity / G1 to G0 transition / IRE1-RACK1-PP2A complex / positive regulation of Golgi to plasma membrane protein transport / TNFR1-mediated ceramide production / negative regulation of formation of translation preinitiation complex / positive regulation of ubiquitin-protein transferase activity / GAIT complex / nucleolus organization / positive regulation of DNA-templated transcription initiation / negative regulation of RNA splicing / negative regulation of DNA repair / TORC2 complex binding / positive regulation of DNA damage response, signal transduction by p53 class mediator / erythrocyte homeostasis / supercoiled DNA binding / regulation of establishment of cell polarity / cysteine-type endopeptidase activator activity involved in apoptotic process / oxidized purine DNA binding / NF-kappaB complex / cytoplasmic translational initiation / rRNA modification in the nucleus and cytosol / negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide / negative regulation of phagocytosis / negative regulation of bicellular tight junction assembly / ubiquitin-like protein conjugating enzyme binding / cytoplasmic side of rough endoplasmic reticulum membrane / Formation of the ternary complex, and subsequently, the 43S complex / laminin receptor activity / negative regulation of myoblast fusion / ion channel inhibitor activity / positive regulation of mitochondrial depolarization / protein kinase A binding / Ribosomal scanning and start codon recognition / Translation initiation complex formation / negative regulation of Wnt signaling pathway / fibroblast growth factor binding / Protein hydroxylation / TOR signaling / negative regulation of translational frameshifting / BH3 domain binding / iron-sulfur cluster binding / monocyte chemotaxis / PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA / mTORC1-mediated signalling / gastrulation / SARS-CoV-1 modulates host translation machinery / regulation of cell division / protein localization to nucleus / positive regulation of GTPase activity / Peptide chain elongation / cellular response to ethanol / protein targeting / Selenocysteine synthesis / Formation of a pool of free 40S subunits / negative regulation of protein binding / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / protein serine/threonine kinase inhibitor activity / negative regulation of respiratory burst involved in inflammatory response / Eukaryotic Translation Termination / Dengue Virus Attachment and Entry / negative regulation of ubiquitin-dependent protein catabolic process / ubiquitin ligase inhibitor activity / SRP-dependent cotranslational protein targeting to membrane Similarity search - Function | ||||||||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.32 Å | ||||||||||||||||||||||||||||||
Authors | Denk, T. / Berninghausen, O. / Beckmann, R. | ||||||||||||||||||||||||||||||
| Funding support | Germany, 1items
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Citation | Journal: Nat Commun / Year: 2026Title: Structural basis of co-translational N-myristoylation in humans. Authors: Timo Denk / Paul Monassa / Joanna Musial / Otto Berninghausen / Birgitta Beatrix / Carmela Giglione / Thierry Meinnel / Roland Beckmann / ![]() Abstract: Modifications of proteins occurring during translation are critical for protein localization, stability and function. N-myristoylation is an essential N-terminal lipid modification catalyzed co- ...Modifications of proteins occurring during translation are critical for protein localization, stability and function. N-myristoylation is an essential N-terminal lipid modification catalyzed co-translationally by N-myristoyltransferases (NMTs) which have been identified as promising drug targets. However, its molecular basis in the context of the translating ribosome is not known. Here, we reveal the structural basis for co-translational N-myristoylation by NMT1 on the human ribosome by cryo-electron microscopy (cryo-EM). We show that NMT1 binds near the peptide tunnel exit and interacts with the nascent polypeptide-associated complex (NAC). Unlike other multi-enzyme complexes that act simultaneously, we find that methionine excision by methionine aminopeptidases and N-myristoylation occur sequentially via consecutive binding to the ribosome. Furthermore, our data suggest that NMT1 remains associated with elongating nascent chains, indicating a co-translational chaperone-like function in partnership with NAC. These insights provide a molecular foundation for the understanding of the co-translational N-myristoylation mechanism in humans. | ||||||||||||||||||||||||||||||
| History |
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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 | 9s3d.cif.gz | 6.7 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9s3d.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9s3d.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/s3/9s3d ftp://data.pdbj.org/pub/pdb/validation_reports/s3/9s3d | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 54530MC ![]() 9i2dC ![]() 9i2eC ![]() 9qloC ![]() 9qlpC ![]() 9qlqC ![]() 9s3bC ![]() 9s3cC 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
-Protein , 11 types, 11 molecules NANBCRCZLILmLsSESeSfSg
| #1: 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: ![]() |
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| #2: Protein | Mass: 17724.037 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: BTF3, NACB, OK/SW-cl.8 / Production host: ![]() |
| #5: Protein | Mass: 49107.734 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: Naturally occurring hydroxylation at K63. / Source: (natural) Homo sapiens (human) / References: UniProt: P62495 |
| #6: Protein | Mass: 10363.395 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) |
| #18: Protein | Mass: 24570.949 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96L21 |
| #47: Protein | Mass: 14758.394 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62987 |
| #52: Protein | Mass: 34309.418 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P05388 |
| #59: Protein | Mass: 29654.869 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62701 |
| #85: Protein | Mass: 14415.724 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62861 |
| #86: Protein | Mass: 18004.041 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62979 |
| #87: Protein | Mass: 35115.652 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P63244 |
-RNA chain , 6 types, 6 molecules CMCPL5L7L8S2
| #3: RNA chain | Mass: 188411.016 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) |
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| #4: RNA chain | Mass: 24189.314 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
| #7: RNA chain | Mass: 1640222.125 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: NR_003287 |
| #8: RNA chain | Mass: 38998.078 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 23898 |
| #9: RNA chain | Mass: 50449.812 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 555853 |
| #54: RNA chain | Mass: 602777.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 151415227 |
+60S ribosomal protein ... , 37 types, 37 molecules LALBLCLDLGLHLJLLLMLNLOLPLQLRLSLTLULVLWLXLYLZLaLbLcLdLeLfLgLh...
-Large ribosomal subunit protein ... , 4 types, 4 molecules LELFLjLt
| #14: Protein | Mass: 32810.176 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q02878 |
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| #15: Protein | Mass: 29290.973 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P18124 |
| #44: Protein | Mass: 11111.032 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P61927 |
| #53: Protein | Mass: 17847.619 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P30050 |
+40S ribosomal protein ... , 29 types, 29 molecules SASBSCSDSFSGSHSISJSKSLSMSNSOSPSQSRSSSTSUSVSWSXSYSZSaSbScSd
-Non-polymers , 3 types, 210 molecules 




| #88: Chemical | ChemComp-MG / #89: Chemical | ChemComp-ZN / #90: 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: NAC bound human RNC with 58 amino acid ARF1-linker / Type: RIBOSOME / Entity ID: #1-#87 / Source: NATURAL |
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| Source (natural) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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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: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 3500 nm / Nominal defocus min: 500 nm |
| Image recording | Electron dose: 40 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.32 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 74754 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||
| Displacement parameters | Biso mean: 123.09 Å2 | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi




Homo sapiens (human)
Germany, 1items
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