+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-50642 | |||||||||
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Title | Human NatA-NAC-MAP1 80S ribosome complex | |||||||||
Map data | ||||||||||
Sample |
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Keywords | co-translational processing / ribosome associated factor (RAF) / methionine aminopeptidase 2 (MAP2) / N-terminal methionine excision (NME) / N-acetyl-transferase A (NatA) / N-termional acetylation (NTA) / UBA domain / a-solenoid / protein-protein and protein-RNA interactions / TRANSLATION | |||||||||
Function / homology | Function and homology information negative regulation of maintenance of mitotic sister chromatid cohesion, centromeric / nascent polypeptide-associated complex / negative regulation of protein localization to endoplasmic reticulum / negative regulation of striated muscle cell apoptotic process / regulation of skeletal muscle fiber development / peptide-glutamate-alpha-N-acetyltransferase activity / N-terminal amino-acid Nalpha-acetyltransferase NatA / positive regulation of cell proliferation involved in heart morphogenesis / N-terminal protein amino acid acetylation / peptide-serine-alpha-N-acetyltransferase activity ...negative regulation of maintenance of mitotic sister chromatid cohesion, centromeric / nascent polypeptide-associated complex / negative regulation of protein localization to endoplasmic reticulum / negative regulation of striated muscle cell apoptotic process / regulation of skeletal muscle fiber development / peptide-glutamate-alpha-N-acetyltransferase activity / N-terminal amino-acid Nalpha-acetyltransferase NatA / positive regulation of cell proliferation involved in heart morphogenesis / N-terminal protein amino acid acetylation / peptide-serine-alpha-N-acetyltransferase activity / NatA complex / positive regulation of skeletal muscle tissue growth / cardiac ventricle development / peptide alpha-N-acetyltransferase activity / N-terminal protein amino acid modification / peptidyl-methionine modification / N-acetyltransferase activity / heart trabecula morphogenesis / methionyl aminopeptidase / initiator methionyl aminopeptidase activity / eukaryotic 80S initiation complex / translation at presynapse / axial mesoderm development / skeletal muscle tissue regeneration / metalloexopeptidase activity / 90S preribosome assembly / TORC2 complex binding / middle ear morphogenesis / alpha-beta T cell differentiation / protein acetylation / internal protein amino acid acetylation / metalloaminopeptidase activity / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / protein maturation / Response of EIF2AK4 (GCN2) to amino acid deficiency / SRP-dependent cotranslational protein targeting to membrane / Viral mRNA Translation / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / GTP hydrolysis and joining of the 60S ribosomal subunit / L13a-mediated translational silencing of Ceruloplasmin expression / chromosome organization / Major pathway of rRNA processing in the nucleolus and cytosol / protein-RNA complex assembly / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / aminopeptidase activity / rough endoplasmic reticulum / cytosolic ribosome / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ossification / ribosomal large subunit biogenesis / skeletal system development / sensory perception of sound / wound healing / platelet aggregation / Regulation of expression of SLITs and ROBOs / cytoplasmic ribonucleoprotein granule / Inactivation, recovery and regulation of the phototransduction cascade / protein transport / ribosome binding / regulation of translation / presynapse / heparin binding / cell body / ribosomal large subunit assembly / cytoplasmic translation / angiogenesis / cytosolic large ribosomal subunit / in utero embryonic development / transcription regulator complex / transcription coactivator activity / postsynaptic density / cell differentiation / protein stabilization / nuclear body / rRNA binding / structural constituent of ribosome / cadherin binding / translation / ribonucleoprotein complex / intracellular membrane-bounded organelle / focal adhesion / mRNA binding / glutamatergic synapse / dendrite / synapse / regulation of DNA-templated transcription / negative regulation of apoptotic process / nucleolus / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / proteolysis / DNA binding / RNA binding / extracellular exosome / identical protein binding / membrane Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.67 Å | |||||||||
Authors | Klein MA / Wild K / Sinning I | |||||||||
Funding support | Germany, 1 items
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Citation | Journal: Nat Commun / Year: 2024 Title: Multi-protein assemblies orchestrate co-translational enzymatic processing on the human ribosome. Authors: Marius Klein / Klemens Wild / Irmgard Sinning / Abstract: Nascent chains undergo co-translational enzymatic processing as soon as their N-terminus becomes accessible at the ribosomal polypeptide tunnel exit (PTE). In eukaryotes, N-terminal methionine ...Nascent chains undergo co-translational enzymatic processing as soon as their N-terminus becomes accessible at the ribosomal polypeptide tunnel exit (PTE). In eukaryotes, N-terminal methionine excision (NME) by Methionine Aminopeptidases (MAP1 and MAP2), and N-terminal acetylation (NTA) by N-Acetyl-Transferase A (NatA), is the most common combination of subsequent modifications carried out on the 80S ribosome. How these enzymatic processes are coordinated in the context of a rapidly translating ribosome has remained elusive. Here, we report two cryo-EM structures of multi-enzyme complexes assembled on vacant human 80S ribosomes, indicating two routes for NME-NTA. Both assemblies form on the 80S independent of nascent chain substrates. Irrespective of the route, NatA occupies a non-intrusive 'distal' binding site on the ribosome which does not interfere with MAP1 or MAP2 binding nor with most other ribosome-associated factors (RAFs). NatA can partake in a coordinated, dynamic assembly with MAP1 through the hydra-like chaperoning function of the abundant Nascent Polypeptide-Associated Complex (NAC). In contrast to MAP1, MAP2 completely covers the PTE and is thus incompatible with NAC and MAP1 recruitment. Together, our data provide the structural framework for the coordinated orchestration of NME and NTA in protein biogenesis. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_50642.map.gz | 509.3 MB | EMDB map data format | |
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Header (meta data) | emd-50642-v30.xml emd-50642.xml | 35 KB 35 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_50642_fsc.xml | 21.3 KB | Display | FSC data file |
Images | emd_50642.png | 67.7 KB | ||
Filedesc metadata | emd-50642.cif.gz | 10.5 KB | ||
Others | emd_50642_half_map_1.map.gz emd_50642_half_map_2.map.gz | 929.1 MB 929.2 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-50642 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-50642 | HTTPS FTP |
-Validation report
Summary document | emd_50642_validation.pdf.gz | 1.2 MB | Display | EMDB validaton report |
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Full document | emd_50642_full_validation.pdf.gz | 1.2 MB | Display | |
Data in XML | emd_50642_validation.xml.gz | 31.3 KB | Display | |
Data in CIF | emd_50642_validation.cif.gz | 41.8 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-50642 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-50642 | HTTPS FTP |
-Related structure data
Related structure data | 9fq0MC 9fpzC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_50642.map.gz / Format: CCP4 / Size: 1000 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.223 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_50642_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_50642_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
+Entire : Human NatA-NAC-MAP1 80S ribosome complex
+Supramolecule #1: Human NatA-NAC-MAP1 80S ribosome complex
+Macromolecule #1: 5.8S rRNA
+Macromolecule #4: 28S rRNA
+Macromolecule #2: Methionine aminopeptidase 1
+Macromolecule #3: Transcription factor BTF3
+Macromolecule #5: Large ribosomal subunit protein uL24
+Macromolecule #6: 60S ribosomal protein L35
+Macromolecule #7: 60S ribosomal protein L23a
+Macromolecule #8: Nascent polypeptide-associated complex subunit alpha
+Macromolecule #9: 60S ribosomal protein L22
+Macromolecule #10: 60S ribosomal protein L19
+Macromolecule #11: 60S ribosomal protein L38
+Macromolecule #12: N-alpha-acetyltransferase 10
+Macromolecule #13: N-alpha-acetyltransferase 15, NatA auxiliary subunit
+Macromolecule #14: 60S ribosomal protein L4
+Macromolecule #15: Large ribosomal subunit protein eL6
+Macromolecule #16: 60S ribosomal protein L28
+Macromolecule #17: INOSITOL HEXAKISPHOSPHATE
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | TFS GLACIOS |
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Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 53.97 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.7 µm / Nominal defocus min: 0.7000000000000001 µm |