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- EMDB-50127: Mammalian ternary complex of a translating 80S ribosome, NAC and ... -

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Entry
Database: EMDB / ID: EMD-50127
TitleMammalian ternary complex of a translating 80S ribosome, NAC and NatA/E - local refinement
Map datamap of the ternary RNC-NAC-NatAE complex refined with a mask on the core of NatA/E
Sample
  • Complex: Ternary complex of a translating ribosome, NAC and NatA/E
    • Complex: Rabbit ribosome-nascent chain complex
    • Complex: Human NAC heterodimer
    • Complex: Human NatA/E complex
      • Complex: Human NatA
      • Complex: Human NatE
Keywordstranslation / ribosome / N-terminal acetyltransferase / NatA / NatE / NAC
Biological speciesOryctolagus cuniculus (rabbit) / Homo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 6.45 Å
AuthorsYudin D / Scaiola A / Ban N
Funding support United States, Germany, Switzerland, European Union, 5 items
OrganizationGrant numberCountry
National Institutes of Health/Office of the DirectorR35 GM136321 United States
German Research Foundation (DFG)SFB969/A01 and A07 Germany
Swiss National Science Foundation310030_212308 Switzerland
Swiss National Science Foundation51NF40-205601 Switzerland
European Research Council (ERC)Synergy Grant 101072047European Union
CitationJournal: Nature / Year: 2024
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
DepositionApr 18, 2024-
Header (metadata) releaseSep 4, 2024-
Map releaseSep 4, 2024-
UpdateOct 2, 2024-
Current statusOct 2, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_50127.png

Downloads & links

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Map

FileDownload / File: emd_50127.map.gz / Format: CCP4 / Size: 669.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationmap of the ternary RNC-NAC-NatAE complex refined with a mask on the core of NatA/E
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.06 Å/pix.
x 560 pix.
= 593.6 Å		1.06 Å/pix.
x 560 pix.
= 593.6 Å		1.06 Å/pix.
x 560 pix.
= 593.6 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.06 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.175
Minimum - Maximum-0.10773797 - 0.51250696
Average (Standard dev.)0.002758405 (±0.028779192)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions560560560
Spacing560560560
CellA=B=C: 593.6 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_50127_msk_1.map
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AxesZYX

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Mask #2

Fileemd_50127_msk_2.map
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Additional map: resampled main map used during the refinement of...

Fileemd_50127_additional_1.map
Annotationresampled main map used during the refinement of the ternary complex model - see the methods section of the manuscript for details
Projections & Slices
AxesZYX

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Half map: halfmap A

Fileemd_50127_half_map_1.map
Annotationhalfmap A
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram

Histogram (log scale)

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Half map: halfmap B

Fileemd_50127_half_map_2.map
Annotationhalfmap B
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Sample components

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Entire : Ternary complex of a translating ribosome, NAC and NatA/E

EntireName: Ternary complex of a translating ribosome, NAC and NatA/E
Components
  • Complex: Ternary complex of a translating ribosome, NAC and NatA/E
    • Complex: Rabbit ribosome-nascent chain complex
    • Complex: Human NAC heterodimer
    • Complex: Human NatA/E complex
      • Complex: Human NatA
      • Complex: Human NatE

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Supramolecule #1: Ternary complex of a translating ribosome, NAC and NatA/E

SupramoleculeName: Ternary complex of a translating ribosome, NAC and NatA/E
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#89
Source (natural)Organism: Oryctolagus cuniculus (rabbit)

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Supramolecule #2: Rabbit ribosome-nascent chain complex

SupramoleculeName: Rabbit ribosome-nascent chain complex / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #2-#10, #13-#74, #76-#79, #81-#89
Source (natural)Organism: Oryctolagus cuniculus (rabbit)

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Supramolecule #3: Human NAC heterodimer

SupramoleculeName: Human NAC heterodimer / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #1, #75
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #4: Human NatA/E complex

SupramoleculeName: Human NatA/E complex / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #11-#12, #80
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #5: Human NatA

SupramoleculeName: Human NatA / type: complex / ID: 5 / Parent: 4 / Macromolecule list: #12, #80
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #6: Human NatE

SupramoleculeName: Human NatE / type: complex / ID: 6 / Parent: 4 / Macromolecule list: #11
Source (natural)Organism: Homo sapiens (human)

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE-PROPANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination 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

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Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 6.45 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 37182
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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