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Open data
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Basic information
| Entry | Database: PDB / ID: 30hi | |||||||||
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| Title | Ternary complex of translating ribosome, NAC and NatB | |||||||||
Components |
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Keywords | TRANSLATION / Cotranslational N-terminal acetylation / N-terminal acetyltransferase B (NaTB) / nascent polypeptide-associated complex (NAC) / translating ribosome | |||||||||
| Function / homology | Function and homology informationN-terminal peptidyl-glutamine acetylation / N-terminal methionine Nalpha-acetyltransferase NatB / N-terminal peptidyl-aspartic acid acetylation / N-terminal peptidyl-glutamic acid acetylation / NatB complex / N-terminal protein amino acid acetylation / protein N-terminal-methionine acetyltransferase activity / regulation of skeletal muscle fiber development / positive regulation of skeletal muscle tissue growth / protein-N-terminal amino-acid acetyltransferase activity ...N-terminal peptidyl-glutamine acetylation / N-terminal methionine Nalpha-acetyltransferase NatB / N-terminal peptidyl-aspartic acid acetylation / N-terminal peptidyl-glutamic acid acetylation / NatB complex / N-terminal protein amino acid acetylation / protein N-terminal-methionine acetyltransferase activity / regulation of skeletal muscle fiber development / positive regulation of skeletal muscle tissue growth / protein-N-terminal amino-acid acetyltransferase activity / positive regulation of cell proliferation involved in heart morphogenesis / cardiac ventricle development / negative regulation of protein localization to endoplasmic reticulum / nascent polypeptide-associated complex / heart trabecula morphogenesis / acetyltransferase activator activity / skeletal muscle tissue regeneration / embryonic brain development / translation at presynapse / response to insecticide / negative regulation of endoplasmic reticulum unfolded protein response / eukaryotic 80S initiation complex / ribosomal protein import into nucleus / regulation of G1 to G0 transition / oxidized pyrimidine DNA binding / response to TNF agonist / positive regulation of base-excision repair / positive regulation of respiratory burst involved in inflammatory response / regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage / positive regulation of gastrulation / protein tyrosine kinase inhibitor activity / IRE1-RACK1-PP2A complex / TNFR1-mediated ceramide production / positive regulation of Golgi to plasma membrane protein transport / G1 to G0 transition / negative regulation of formation of translation preinitiation complex / nucleolus organization / positive regulation of ubiquitin-protein transferase activity / negative regulation of RNA splicing / GAIT complex / positive regulation of DNA-templated transcription initiation / negative regulation of DNA repair / negative regulation of striated muscle cell apoptotic process / TORC2 complex binding / erythrocyte homeostasis / supercoiled DNA binding / regulation of establishment of cell polarity / rRNA modification in the nucleus and cytosol / oxidized purine DNA binding / NF-kappaB complex / negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide / negative regulation of phagocytosis / ubiquitin-like protein conjugating enzyme binding / cytoplasmic translational initiation / cytoplasmic side of rough endoplasmic reticulum membrane / regulation of translation involved in cellular response to UV / A band / Formation of the ternary complex, and subsequently, the 43S complex / ion channel inhibitor activity / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / laminin receptor activity / response to aldosterone / negative regulation of myoblast fusion / protein-DNA complex disassembly / Ribosomal scanning and start codon recognition / protein kinase A binding / Translation initiation complex formation / negative regulation of Wnt signaling pathway / positive regulation of DNA damage response, signal transduction by p53 class mediator / fibroblast growth factor binding / BH3 domain binding / Protein hydroxylation / TOR signaling / mTORC1-mediated signalling / negative regulation of translational frameshifting / monocyte chemotaxis / PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA / SARS-CoV-1 modulates host translation machinery / regulation of cell division / positive regulation of GTPase activity / protein localization to nucleus / Peptide chain elongation / Selenocysteine synthesis / negative regulation of protein binding / Formation of a pool of free 40S subunits / negative regulation of respiratory burst involved in inflammatory response / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / protein serine/threonine kinase inhibitor activity / protein targeting / Eukaryotic Translation Termination / Dengue Virus Attachment and Entry / SRP-dependent cotranslational protein targeting to membrane / Response of EIF2AK4 (GCN2) to amino acid deficiency / Viral mRNA Translation / endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ubiquitin ligase inhibitor activity / 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 Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å | |||||||||
Authors | Knejski, P. / Scaiola, A. / Leibundgut, M. / Ban, N. | |||||||||
| Funding support | Switzerland, European Union, 2items
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Citation | Journal: Nat Commun / Year: 2026Title: Structural basis of cotranslational protein N-terminal acetylation by NatB in human cells. Authors: Natalia Silva Alves / Pawel Knejski / Alain Scaiola / Marc Leibundgut / Martin Gamerdinger / Nenad Ban / Elke Deuerling / ![]() Abstract: Cotranslational N-terminal acetylation is a widespread modification that shapes protein stability, localization, and function in eukaryotic cells. The essential human NatB complex (NAA25-NAA20) ...Cotranslational N-terminal acetylation is a widespread modification that shapes protein stability, localization, and function in eukaryotic cells. The essential human NatB complex (NAA25-NAA20) acetylates the initiator methionine of a substantial fraction of the proteome, yet how NatB engages translating ribosomes has remained unclear. Here we define the cotranslational mechanism underlying NatB function. NatB is recruited by the nascent polypeptide-associated complex (NAC) through a high-affinity interaction between the NACα UBA domain and the auxiliary subunit NAA25, while both NatB subunits form additional contacts with the ribosomal surface near the tunnel exit. Together, these interactions position the NatB active site directly adjacent to the emerging nascent chain, enabling efficient modification of newly synthesized proteins. Structural comparisons reveal a conserved ribosome-binding architecture shared with other N-acetyltransferases, including NatA/E and NatD, implying mutually exclusive ribosome occupancy. Together with prior work, these findings establish NAC as a central organizer of cotranslational N-terminal processing. | |||||||||
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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 | 30hi.cif.gz | 5.8 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb30hi.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 30hi.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/0h/30hi ftp://data.pdbj.org/pub/pdb/validation_reports/0h/30hi | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 57771MC 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 , 8 types, 8 molecules B1BmBsBuBvAeAfAg
| #1: Protein | Mass: 6589.557 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Human ANXA4 sequence with murine N-terminus fused to Xbp1u arrest peptide. N-terminus modeled as poly-Alanine and Glycine string Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) |
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| #44: Protein | Mass: 14758.394 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62987 |
| #48: Protein | Mass: 34309.418 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P05388 |
| #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: 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: ![]() |
| #86: Protein | Mass: 14415.724 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62861 |
| #87: Protein | Mass: 18004.041 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62979 |
| #88: 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 B2B4B5B7B8A2
| #2: RNA chain | Mass: 24708.902 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: chr8:123157230-123157302 (-) / Source: (natural) Homo sapiens (human) |
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| #3: RNA chain | Mass: 1877.157 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: mRNA in vitro transcribed using T7 polymerase / Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) |
| #4: RNA chain | Mass: 1640856.500 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
| #5: RNA chain | Mass: 38346.707 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 23898 |
| #6: RNA chain | Mass: 50477.867 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 2033716901 |
| #55: RNA chain | Mass: 603622.250 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
-Large ribosomal subunit protein ... , 11 types, 11 molecules BABBBEBFBaBbBfBjBoBrBt
| #7: Protein | Mass: 28103.855 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62917 |
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| #8: Protein | Mass: 46224.133 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P39023 |
| #11: Protein | Mass: 32810.176 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q02878 |
| #12: Protein | Mass: 29290.973 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P18124 |
| #32: Protein | Mass: 16619.527 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P46776 |
| #33: Protein | Mass: 17817.295 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P47914 |
| #37: Protein | Mass: 12564.743 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P18077 |
| #41: Protein | Mass: 11111.032 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P61927 |
| #45: Protein | Mass: 12489.991 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P83881 |
| #47: Protein | Mass: 15679.466 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P46779 |
| #49: Protein | Mass: 17847.619 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P30050 |
+60S ribosomal protein ... , 32 types, 32 molecules BCBDBGBHBIBJBLBMBNBOBPBQBRBSBTBUBVBWBXBYBZBcBdBeBgBhBiBkBlBpBzAh
-N-alpha-acetyltransferase ... , 2 types, 2 molecules BwBy
| #52: Protein | Mass: 113273.156 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: The N-terminus of the protein contains a hexahistidine tag Source: (gene. exp.) Homo sapiens (human) / Gene: NAA25, C12orf30, MDM20, NAP1 / Production host: ![]() |
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| #53: Protein | Mass: 20390.133 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NAA20, NAT5 / Production host: ![]() References: UniProt: P61599, N-terminal methionine Nalpha-acetyltransferase NatB |
-Small ribosomal subunit protein ... , 8 types, 8 molecules AAAEALASATAVAXAZ
| #56: Protein | Mass: 32778.777 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P08865 |
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| #60: Protein | Mass: 29654.869 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62701 |
| #67: Protein | Mass: 18468.826 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62280 |
| #74: Protein | Mass: 17654.619 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62269 |
| #75: Protein | Mass: 16104.579 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P39019 |
| #77: Protein | Mass: 9150.427 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P63220 |
| #79: Protein | Mass: 15860.666 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62266 |
| #81: Protein | Mass: 13776.224 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62851 |
+40S ribosomal protein ... , 22 types, 22 molecules ABACADAFAGAHAIAJAKAMANAOAPAQARAUAWAYAaAbAcAd
-Non-polymers , 4 types, 463 molecules 






| #90: Chemical | ChemComp-MG / #91: Chemical | ChemComp-GTP / | #92: Chemical | ChemComp-ZN / #93: Chemical | ChemComp-COA / | |
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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: 7.5 | ||||||||||||||||||||||||||||||||||||
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||||||||
| Vitrification | 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: 2400 nm / Nominal defocus min: 900 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||
| 3D reconstruction | Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 63788 / Symmetry type: POINT |
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About Yorodumi




Homo sapiens (human)
Switzerland, European Union, 2items
Citation


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FIELD EMISSION GUN