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Yorodumi- PDB-9qqb: Quaternary complex of a translating ribosome, NAC, NMT1, and NatA -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9qqb | ||||||||||||
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| Title | Quaternary complex of a translating ribosome, NAC, NMT1, and NatA | ||||||||||||
Components |
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Keywords | RIBOSOME / Translation / co-translational protein processing | ||||||||||||
| Function / homology | Function and homology informationnegative regulation of maintenance of mitotic sister chromatid cohesion, centromeric / negative regulation of protein localization to endoplasmic reticulum / nascent polypeptide-associated complex / [histone H4]-N-methyl-L-lysine20 N-methyltransferase / negative regulation of striated muscle cell apoptotic process / protein-N-terminal-glutamate acetyltransferase activity / regulation of skeletal muscle fiber development / N-terminal amino-acid Nalpha-acetyltransferase NatA / N-terminal protein amino acid acetylation / myristoyltransferase activity ...negative regulation of maintenance of mitotic sister chromatid cohesion, centromeric / negative regulation of protein localization to endoplasmic reticulum / nascent polypeptide-associated complex / [histone H4]-N-methyl-L-lysine20 N-methyltransferase / negative regulation of striated muscle cell apoptotic process / protein-N-terminal-glutamate acetyltransferase activity / regulation of skeletal muscle fiber development / N-terminal amino-acid Nalpha-acetyltransferase NatA / N-terminal protein amino acid acetylation / myristoyltransferase activity / positive regulation of cell proliferation involved in heart morphogenesis / [histone H4]-lysine20 N-methyltransferase / N-terminal peptidyl-glycine N-myristoylation / peptidyl-lysine N6-myristoyltransferase activity / NatA complex / positive regulation of skeletal muscle tissue growth / protein N-terminal-serine acetyltransferase activity / Late Phase of HIV Life Cycle / protein-N-terminal-alanine acetyltransferase activity / ketone metabolic process / histone H4K20 methyltransferase activity / regulation of opsin-mediated signaling pathway / protein-N-terminal amino-acid acetyltransferase activity / internal protein amino acid acetylation / cardiac ventricle development / Activation, myristolyation of BID and translocation to mitochondria / positive regulation of establishment of protein localization to mitochondrion / glycylpeptide N-tetradecanoyltransferase / glycylpeptide N-tetradecanoyltransferase activity / heart trabecula morphogenesis / N-acetyltransferase activity / skeletal muscle tissue regeneration / acetyltransferase activator activity / ribosomal subunit / S-adenosyl-L-methionine binding / protein localization to membrane / protein acetylation / laminin receptor activity / positive regulation of double-strand break repair via nonhomologous end joining / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / ubiquitin ligase inhibitor activity / SRP-dependent cotranslational protein targeting to membrane / Response of EIF2AK4 (GCN2) to amino acid deficiency / positive regulation of signal transduction by p53 class mediator / Viral mRNA Translation / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / 90S preribosome / GTP hydrolysis and joining of the 60S ribosomal subunit / chromosome organization / L13a-mediated translational silencing of Ceruloplasmin expression / Major pathway of rRNA processing in the nucleolus and cytosol / phagocytic cup / pericentric heterochromatin / protein-RNA complex assembly / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / maturation of LSU-rRNA / laminin binding / rough endoplasmic reticulum / eNOS activation / translation regulator activity / ribosomal small subunit export from nucleus / gastrulation / MDM2/MDM4 family protein binding / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / cytosolic ribosome / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / DNA-(apurinic or apyrimidinic site) lyase / ribosomal large subunit biogenesis / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / positive regulation of apoptotic signaling pathway / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / small-subunit processome / wound healing / Regulation of expression of SLITs and ROBOs / spindle / cytoplasmic ribonucleoprotein granule / rRNA processing / antimicrobial humoral immune response mediated by antimicrobial peptide / rhythmic process / positive regulation of canonical Wnt signaling pathway / Inactivation, recovery and regulation of the phototransduction cascade / heparin binding / regulation of translation / protein transport / large ribosomal subunit / ribosome binding / virus receptor activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / angiogenesis Similarity search - Function | ||||||||||||
| Biological species | Homo sapiens (human)![]() | ||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.43 Å | ||||||||||||
Authors | Echeverria, B. / Jaskolowski, M. / Scaiola, A. / Ban, N. | ||||||||||||
| Funding support | Switzerland, European Union, 3items
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Citation | Journal: Mol Cell / Year: 2025Title: Mechanism of cotranslational protein N-myristoylation in human cells. Authors: Martin Gamerdinger / Blanca Echeverria / Alfred M Lentzsch / Nicolas Burg / Ziyi Fan / Mateusz Jaskolowski / Alain Scaiola / Selina Piening / Shu-Ou Shan / Nenad Ban / Elke Deuerling / ![]() Abstract: N-myristoyltransferases (NMTs) cotranslationally transfer the fatty acid myristic acid to the N terminus of newly synthesized proteins, regulating their function and cellular localization. These ...N-myristoyltransferases (NMTs) cotranslationally transfer the fatty acid myristic acid to the N terminus of newly synthesized proteins, regulating their function and cellular localization. These enzymes are important drug targets for the treatment of cancer and viral infections. N-myristoylation of nascent proteins occurs specifically on N-terminal glycine residues after the excision of the initiator methionine by methionine aminopeptidases (METAPs). How NMTs interact with ribosomes and gain timely and specific access to their substrates remains unknown. Here, we show that human NMT1 exchanges with METAP1 at the ribosomal tunnel exit to form an active cotranslational complex together with the nascent polypeptide-associated complex (NAC). NMT1 binding is sequence selective and specifically triggered by methionine excision, which exposes the N-myristoylation motif in the nascent chain. The revealed mode of interaction of NMT1 with NAC and the methionine-cleaved nascent protein elucidates how a specific subset of proteins can be efficiently N-myristoylated in human cells. | ||||||||||||
| 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 | 9qqb.cif.gz | 6.6 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9qqb.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9qqb.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9qqb_validation.pdf.gz | 2.7 MB | Display | wwPDB validaton report |
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| Full document | 9qqb_full_validation.pdf.gz | 3 MB | Display | |
| Data in XML | 9qqb_validation.xml.gz | 454.1 KB | Display | |
| Data in CIF | 9qqb_validation.cif.gz | 750.1 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qq/9qqb ftp://data.pdbj.org/pub/pdb/validation_reports/qq/9qqb | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 53296MC ![]() 9qqaC 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 , 5 types, 5 molecules B5B7B8A2AT
+Large ribosomal subunit protein ... , 10 types, 10 molecules BABCBDBLBOBPBSBXBoBs
+Ribosomal protein ... , 10 types, 10 molecules BBBFBNBRBVBWBYBeBjBv
+60S ribosomal protein ... , 21 types, 21 molecules BEBGBHBIBJBMBTBUBZBaBbBcBdBfBgBhBiBkBlBpBt
+Protein/peptide , 1 types, 1 molecules BK
+Protein , 8 types, 8 molecules BQBrNtNuMAADAEAj
+Ubiquitin-ribosomal protein ... , 2 types, 2 molecules BmAC
+N-alpha-acetyltransferase ... , 2 types, 2 molecules XAXB
+Small ribosomal subunit protein ... , 20 types, 20 molecules AAABAFAGAZAeAiAkAlAmAnAoApAqArAtAuAvAyAz
+40S ribosomal protein ... , 10 types, 10 molecules AaAbAcAdAfAgAhAsAwAx
+Non-polymers , 7 types, 2696 molecules 












+Details
-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: Quaternary complex of translating ribosome, NAC, NMT1 and NatA Type: RIBOSOME / Entity ID: #1-#13, #15-#89 / Source: NATURAL |
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| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.6 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE-PROPANE |
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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: 2700 nm / Nominal defocus min: 700 nm |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.21.2_5419 / Category: model refinement |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
| 3D reconstruction | Resolution: 3.43 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 15709 / Symmetry type: POINT |
| Refinement | Cross valid method: NONE |
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About Yorodumi



Homo sapiens (human)

Switzerland, European Union, 3items
Citation




PDBj




















































FIELD EMISSION GUN