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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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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 / positive regulation of protein refolding / [histone H4]-N-methyl-L-lysine20 N-methyltransferase / protein-N-terminal-glutamate acetyltransferase activity / N-terminal amino-acid Nalpha-acetyltransferase NatA / [histone H4]-lysine20 N-methyltransferase / histone H4K20 monomethyltransferase activity / NatA complex / myristoyltransferase activity / protein myristoylation ...negative regulation of maintenance of mitotic sister chromatid cohesion, centromeric / positive regulation of protein refolding / [histone H4]-N-methyl-L-lysine20 N-methyltransferase / protein-N-terminal-glutamate acetyltransferase activity / N-terminal amino-acid Nalpha-acetyltransferase NatA / [histone H4]-lysine20 N-methyltransferase / histone H4K20 monomethyltransferase activity / NatA complex / myristoyltransferase activity / protein myristoylation / peptidyl-lysine N6-myristoyltransferase activity / CoA-dependent peptidyl-lysine N6-myristoyltransferase activity / protein-N-terminal-alanine acetyltransferase activity / Late Phase of HIV Life Cycle / N-terminal protein myristoylation / histone H4K20me methyltransferase activity / protein N-terminal-serine acetyltransferase activity / N-terminal peptidyl-glycine N-myristoylation / regulation of skeletal muscle fiber development / ketone metabolic process / positive regulation of skeletal muscle tissue growth / protein-N-terminal amino-acid acetyltransferase activity / regulation of opsin-mediated signaling pathway / positive regulation of cell proliferation involved in heart morphogenesis / cardiac ventricle development / Activation, myristolyation of BID and translocation to mitochondria / negative regulation of protein localization to endoplasmic reticulum / nascent polypeptide-associated complex / heart trabecula morphogenesis / glycylpeptide N-tetradecanoyltransferase / glycylpeptide N-tetradecanoyltransferase activity / N-acetyltransferase activity / acetyltransferase activator activity / skeletal muscle tissue regeneration / protein-RNA complex assembly / S-adenosyl-L-methionine binding / protein localization to membrane / negative regulation of striated muscle cell apoptotic process / positive regulation of double-strand break repair via nonhomologous end joining / positive regulation of protein localization to mitochondrion / regulation of translation involved in cellular response to UV / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / laminin receptor activity / negative regulation of myoblast fusion / protein-DNA complex disassembly / positive regulation of DNA damage response, signal transduction by p53 class mediator / PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / pericentric heterochromatin / Eukaryotic Translation Termination / SRP-dependent cotranslational protein targeting to membrane / Response of EIF2AK4 (GCN2) to amino acid deficiency / Viral mRNA Translation / ubiquitin ligase inhibitor activity / 90S preribosome / 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 / eNOS activation / negative regulation of ubiquitin-dependent protein catabolic process / translation regulator activity / ribosomal small subunit export from nucleus / rough endoplasmic reticulum / laminin binding / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / positive regulation of apoptotic signaling pathway / MDM2/MDM4 family protein binding / wound healing / DNA-(apurinic or apyrimidinic site) lyase / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ribosome stalled on a no-go mRNA / ribosomal large subunit biogenesis / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / DNA damage response, signal transduction by p53 class mediator / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / striated muscle contraction / Maturation of DENV proteins / positive regulation of translation / small-subunit processome / cellular response to gamma radiation / Dengue Virus Genome Translation and Replication / protein maturation / spindle / Regulation of expression of SLITs and ROBOs / cytoplasmic ribonucleoprotein granule / mRNA 5'-UTR binding / rRNA processing / Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide / transcription coactivator binding / cytosolic ribosome / glucose homeostasis / large ribosomal subunit 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
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qq/9qqb ftp://data.pdbj.org/pub/pdb/validation_reports/qq/9qqb | HTTPS FTP |
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-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




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FIELD EMISSION GUN