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- EMDB-50124: Mammalian ternary complex of a translating 80S ribosome, NAC and ... -
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Basic information
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Title | Mammalian ternary complex of a translating 80S ribosome, NAC and NatA/E | ||||||||||||||||||
![]() | homogeneously refined cryo-EM map of the ternary RNC-NAC-NatA/E complex | ||||||||||||||||||
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![]() | translation / ribosome / N-terminal acetyltransferase / NatA / NatE / NAC | ||||||||||||||||||
Function / homology | ![]() negative regulation of maintenance of mitotic sister chromatid cohesion, centromeric / negative regulation of protein localization to endoplasmic reticulum / nascent polypeptide-associated complex / negative regulation of striated muscle cell apoptotic process / mitotic sister chromatid cohesion, centromeric / regulation of skeletal muscle fiber development / protein-N-terminal-glutamate acetyltransferase activity / N-terminal methionine Nalpha-acetyltransferase NatE / N-terminal amino-acid Nalpha-acetyltransferase NatA / positive regulation of cell proliferation involved in heart morphogenesis ...negative regulation of maintenance of mitotic sister chromatid cohesion, centromeric / negative regulation of protein localization to endoplasmic reticulum / nascent polypeptide-associated complex / negative regulation of striated muscle cell apoptotic process / mitotic sister chromatid cohesion, centromeric / regulation of skeletal muscle fiber development / protein-N-terminal-glutamate acetyltransferase activity / N-terminal methionine Nalpha-acetyltransferase NatE / N-terminal amino-acid Nalpha-acetyltransferase NatA / positive regulation of cell proliferation involved in heart morphogenesis / N-terminal protein amino acid acetylation / NatA complex / protein N-terminal-serine acetyltransferase activity / protein-N-terminal-alanine acetyltransferase activity / protein N-terminal-methionine acetyltransferase activity / positive regulation of skeletal muscle tissue growth / cardiac ventricle development / protein-N-terminal amino-acid acetyltransferase activity / internal protein amino acid acetylation / acetyltransferase activator activity / N-acetyltransferase activity / histone H4 acetyltransferase activity / heart trabecula morphogenesis / establishment of mitotic sister chromatid cohesion / skeletal muscle tissue regeneration / ribosomal subunit / exit from mitosis / optic nerve development / protein-lysine-acetyltransferase activity / mitotic sister chromatid cohesion / laminin receptor activity / retinal ganglion cell axon guidance / protein acetylation / glutathione transferase / positive regulation of signal transduction by p53 class mediator / ubiquitin ligase inhibitor activity / glutathione transferase activity / phagocytic cup / 90S preribosome / chromosome organization / protein-RNA complex assembly / ribosomal small subunit export from nucleus / rough endoplasmic reticulum / laminin binding / translation regulator activity / gastrulation / MDM2/MDM4 family protein binding / cytosolic ribosome / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / glutathione metabolic process / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / DNA-(apurinic or apyrimidinic site) lyase / cellular response to interleukin-4 / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosomal large subunit biogenesis / 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 / spindle / mRNA 5'-UTR binding / cytoplasmic ribonucleoprotein granule / antimicrobial humoral immune response mediated by antimicrobial peptide / rRNA processing / rhythmic process / positive regulation of canonical Wnt signaling pathway / protein transport / regulation of translation / large ribosomal subunit / heparin binding / ribosome binding / virus receptor activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / retina development in camera-type eye / small ribosomal subunit / 5S rRNA binding / ribosomal large subunit assembly / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / small ribosomal subunit rRNA binding / defense response to Gram-negative bacterium / angiogenesis / killing of cells of another organism / perikaryon / transcription regulator complex / cytosolic large ribosomal subunit / in utero embryonic development / cytoplasmic translation / cell differentiation / transcription coactivator activity / tRNA binding / mitochondrial inner membrane / postsynaptic density / negative regulation of translation / protein stabilization / rRNA binding / nuclear body / ribosome Similarity search - Function | ||||||||||||||||||
Biological species | ![]() ![]() ![]() | ||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.01 Å | ||||||||||||||||||
![]() | Yudin D / Scaiola A / Ban N | ||||||||||||||||||
Funding support | ![]() ![]() ![]()
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![]() | ![]() Title: NAC guides a ribosomal multienzyme complex for nascent protein processing. Authors: Alfred M Lentzsch / Denis Yudin / Martin Gamerdinger / Sowmya Chandrasekar / Laurenz Rabl / Alain Scaiola / Elke Deuerling / Nenad Ban / Shu-Ou Shan / ![]() ![]() ![]() Abstract: Approximately 40% of the mammalian proteome undergoes N-terminal methionine excision and acetylation, mediated sequentially by methionine aminopeptidase (MetAP) and N-acetyltransferase A (NatA), ...Approximately 40% of the mammalian proteome undergoes N-terminal methionine excision and acetylation, mediated sequentially by methionine aminopeptidase (MetAP) and N-acetyltransferase A (NatA), respectively. Both modifications are strictly cotranslational and essential in higher eukaryotic organisms. The interaction, activity and regulation of these enzymes on translating ribosomes are poorly understood. Here we perform biochemical, structural and in vivo studies to demonstrate that the nascent polypeptide-associated complex (NAC) orchestrates the action of these enzymes. NAC assembles a multienzyme complex with MetAP1 and NatA early during translation and pre-positions the active sites of both enzymes for timely sequential processing of the nascent protein. NAC further releases the inhibitory interactions from the NatA regulatory protein huntingtin yeast two-hybrid protein K (HYPK) to activate NatA on the ribosome, enforcing cotranslational N-terminal acetylation. Our results provide a mechanistic model for the cotranslational processing of proteins in eukaryotic cells. | ||||||||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 337.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 135.7 KB 135.7 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 20.8 KB | Display | ![]() |
Images | ![]() | 126.4 KB | ||
Masks | ![]() ![]() | 669.9 MB 669.9 MB | ![]() | |
Filedesc metadata | ![]() | 25.1 KB | ||
Others | ![]() ![]() ![]() ![]() ![]() | 622.8 MB 37.1 MB 625.7 MB 621.2 MB 621.2 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9f1bMC ![]() 9f1cC ![]() 9f1dC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | homogeneously refined cryo-EM map of the ternary RNC-NAC-NatA/E complex | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.06 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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-Additional map: main map lowpass filtered to 8 A resolution
File | emd_50124_additional_1.map | ||||||||||||
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Annotation | main map lowpass filtered to 8 A resolution | ||||||||||||
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-Additional map: main map lowpass filtered to estimated local resolution
File | emd_50124_additional_2.map | ||||||||||||
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Annotation | main map lowpass filtered to estimated local resolution | ||||||||||||
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-Additional map: main map lowpass filtered to 6 A resolution
File | emd_50124_additional_3.map | ||||||||||||
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Annotation | main map lowpass filtered to 6 A resolution | ||||||||||||
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-Half map: halfmap A
File | emd_50124_half_map_1.map | ||||||||||||
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Annotation | halfmap A | ||||||||||||
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-Half map: halfmap B
File | emd_50124_half_map_2.map | ||||||||||||
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Annotation | halfmap B | ||||||||||||
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Sample components
+Entire : Ternary complex of a translating ribosome, NAC and NatA/E
+Supramolecule #1: Ternary complex of a translating ribosome, NAC and NatA/E
+Supramolecule #2: Rabbit ribosome-nascent chain complex
+Supramolecule #3: Human NAC heterodimer
+Supramolecule #4: Human NatA/E complex
+Supramolecule #5: Human NatA
+Supramolecule #6: Human NatE with a GST tag
+Macromolecule #1: Large ribosomal subunit protein uL22
+Macromolecule #2: 40S ribosomal protein eS17
+Macromolecule #3: Large ribosomal subunit protein eL42
+Macromolecule #5: Small ribosomal subunit protein uS13
+Macromolecule #6: Transcription factor BTF3
+Macromolecule #7: Large ribosomal subunit protein eL13
+Macromolecule #8: Ribosomal_L23eN domain-containing protein
+Macromolecule #9: 60S ribosomal protein L37a
+Macromolecule #10: Large ribosomal subunit protein eL18
+Macromolecule #11: 40S ribosomal protein S19
+Macromolecule #12: Large ribosomal subunit protein eL28
+Macromolecule #13: Ribosomal protein L19
+Macromolecule #14: Small ribosomal subunit protein uS10
+Macromolecule #15: 60S acidic ribosomal protein P0
+Macromolecule #16: 60S ribosomal protein L7a
+Macromolecule #17: 60S ribosomal protein L22
+Macromolecule #18: Ribosomal protein S15a
+Macromolecule #19: N-alpha-acetyltransferase 15, NatA auxiliary subunit
+Macromolecule #20: Nascent polypeptide-associated complex subunit alpha
+Macromolecule #21: 60S ribosomal protein L9
+Macromolecule #22: Ribosomal protein L23
+Macromolecule #23: 40S ribosomal protein S23
+Macromolecule #25: 60S ribosomal protein L21
+Macromolecule #26: 60S ribosomal protein L10
+Macromolecule #27: Ribosomal protein L24
+Macromolecule #28: 40S ribosomal protein S24
+Macromolecule #30: Small ribosomal subunit protein eS21
+Macromolecule #31: 60S ribosomal protein L11
+Macromolecule #32: Small ribosomal subunit protein uS2
+Macromolecule #33: 40S ribosomal protein S25
+Macromolecule #35: Nascent chain
+Macromolecule #36: 40S ribosomal protein S3a
+Macromolecule #37: 60S ribosomal protein L41
+Macromolecule #38: Large ribosomal subunit protein uL2
+Macromolecule #39: 60S ribosomal protein L12
+Macromolecule #40: 60S ribosomal protein L14
+Macromolecule #41: 40S ribosomal protein S2
+Macromolecule #42: Ribosomal protein L26
+Macromolecule #43: Ribosomal protein L3
+Macromolecule #44: Large ribosomal subunit protein eL20
+Macromolecule #45: 40S ribosomal protein S3
+Macromolecule #46: 60S ribosomal protein L27
+Macromolecule #47: Large ribosomal subunit protein uL4
+Macromolecule #48: Ribosomal protein L15
+Macromolecule #49: 40S ribosomal protein S4
+Macromolecule #50: 60S ribosomal protein L27a
+Macromolecule #51: Large ribosomal subunit protein uL18
+Macromolecule #52: Large ribosomal subunit protein uL13
+Macromolecule #53: Ribosomal protein S5
+Macromolecule #54: 60S ribosomal protein L29
+Macromolecule #55: 60S ribosomal protein L6
+Macromolecule #56: Glutathione S-transferase class-mu 26 kDa isozyme,N-alpha-acetylt...
+Macromolecule #57: 40S ribosomal protein S6
+Macromolecule #58: 60S ribosomal protein L30
+Macromolecule #59: Ribosomal Protein uL30
+Macromolecule #60: N-alpha-acetyltransferase 10
+Macromolecule #61: 40S ribosomal protein S7
+Macromolecule #62: 60S ribosomal protein L31
+Macromolecule #64: 40S ribosomal protein S8
+Macromolecule #65: Ribosomal protein L32
+Macromolecule #66: 40S ribosomal protein S27
+Macromolecule #67: 40S ribosomal protein S9
+Macromolecule #68: 60S ribosomal protein L35a
+Macromolecule #69: 40S ribosomal protein S28
+Macromolecule #70: S10_plectin domain-containing protein
+Macromolecule #71: Large ribosomal subunit protein eL34
+Macromolecule #72: Ribosomal protein S27a
+Macromolecule #73: 40S ribosomal protein S11
+Macromolecule #74: 60S ribosomal protein L35
+Macromolecule #75: 40S ribosomal protein S30
+Macromolecule #76: 40S ribosomal protein S12
+Macromolecule #77: 60S ribosomal protein L36
+Macromolecule #78: Small ribosomal subunit protein eS26
+Macromolecule #79: 40S ribosomal protein S13
+Macromolecule #80: Ribosomal protein L37
+Macromolecule #81: Small ribosomal subunit protein RACK1
+Macromolecule #82: Small ribosomal subunit protein uS11
+Macromolecule #83: 60S ribosomal protein L38
+Macromolecule #84: 40S ribosomal protein S29
+Macromolecule #85: 40S ribosomal protein uS19
+Macromolecule #86: 60S ribosomal protein L39-like
+Macromolecule #88: Small ribosomal subunit protein uS9
+Macromolecule #89: Ubiquitin-ribosomal protein eL40 fusion protein
+Macromolecule #4: P-site tRNA
+Macromolecule #24: 28S rRNA
+Macromolecule #29: 5S rRNA
+Macromolecule #34: 5.8S rRNA
+Macromolecule #63: 18S rRNA
+Macromolecule #87: mRNA
+Macromolecule #90: MAGNESIUM ION
+Macromolecule #91: ZINC ION
+Macromolecule #92: UNKNOWN ATOM OR ION
+Macromolecule #93: INOSITOL HEXAKISPHOSPHATE
+Macromolecule #94: SPERMIDINE
+Macromolecule #95: SPERMINE
+Macromolecule #96: GUANOSINE-5'-TRIPHOSPHATE
+Macromolecule #97: water
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE-PROPANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 0.6 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |