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- EMDB-29768: mRNA decoding in human is kinetically and structurally distinct f... -

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Basic information

Entry
Database: EMDB / ID: EMD-29768
TitlemRNA decoding in human is kinetically and structurally distinct from bacteria (40S Focus refined map)
Map dataUnsharpened refine3D map
Sample
  • Complex: Human ribosome
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 1.8 Å
AuthorsHolm M / Natchiar KS / Rundlet EJ / Myasnikov AG / Altman RB / Blanchard SC
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: Nature / Year: 2023
Title: mRNA decoding in human is kinetically and structurally distinct from bacteria.
Authors: Mikael Holm / S Kundhavai Natchiar / Emily J Rundlet / Alexander G Myasnikov / Zoe L Watson / Roger B Altman / Hao-Yuan Wang / Jack Taunton / Scott C Blanchard /
Abstract: In all species, ribosomes synthesize proteins by faithfully decoding messenger RNA (mRNA) nucleotide sequences using aminoacyl-tRNA substrates. Current knowledge of the decoding mechanism derives ...In all species, ribosomes synthesize proteins by faithfully decoding messenger RNA (mRNA) nucleotide sequences using aminoacyl-tRNA substrates. Current knowledge of the decoding mechanism derives principally from studies on bacterial systems. Although key features are conserved across evolution, eukaryotes achieve higher-fidelity mRNA decoding than bacteria. In human, changes in decoding fidelity are linked to ageing and disease and represent a potential point of therapeutic intervention in both viral and cancer treatment. Here we combine single-molecule imaging and cryogenic electron microscopy methods to examine the molecular basis of human ribosome fidelity to reveal that the decoding mechanism is both kinetically and structurally distinct from that of bacteria. Although decoding is globally analogous in both species, the reaction coordinate of aminoacyl-tRNA movement is altered on the human ribosome and the process is an order of magnitude slower. These distinctions arise from eukaryote-specific structural elements in the human ribosome and in the elongation factor eukaryotic elongation factor 1A (eEF1A) that together coordinate faithful tRNA incorporation at each mRNA codon. The distinct nature and timing of conformational changes within the ribosome and eEF1A rationalize how increased decoding fidelity is achieved and potentially regulated in eukaryotic species.
History
DepositionFeb 15, 2023-
Header (metadata) releaseApr 19, 2023-
Map releaseApr 19, 2023-
UpdateMay 17, 2023-
Current statusMay 17, 2023Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_29768.png

Downloads & links

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Map

FileDownload / File: emd_29768.map.gz / Format: CCP4 / Size: 1000 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationUnsharpened refine3D map
Voxel sizeX=Y=Z: 0.826 Å
Density
Contour LevelBy AUTHOR: 0.005
Minimum - Maximum-0.016124504 - 0.070568874
Average (Standard dev.)4.879719e-05 (±0.001460246)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions640640640
Spacing640640640
CellA=B=C: 528.64 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_29768_msk_1.map
Projections & Slices
AxesZYX

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Additional map: Post-processed map

Fileemd_29768_additional_1.map
AnnotationPost-processed map
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Additional map: Post-processed masked map

Fileemd_29768_additional_2.map
AnnotationPost-processed masked map
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AxesZYX

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Half map: Half map 1

Fileemd_29768_half_map_1.map
AnnotationHalf map 1
Projections & Slices
AxesZYX

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Histogram

Histogram (log scale)

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Half map: Half map 2

Fileemd_29768_half_map_2.map
AnnotationHalf map 2
Projections & Slices
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Sample components

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Entire : Human ribosome

EntireName: Human ribosome
Components
  • Complex: Human ribosome

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Supramolecule #1: Human ribosome

SupramoleculeName: Human ribosome / type: complex / ID: 1 / Chimera: Yes / Parent: 0
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

Concentration4 mg/mL
BufferpH: 7
VitrificationCryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 283 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: -1.5 µm / Nominal defocus min: -0.5 µm
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 79.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 1.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 845750
FSC plot (resolution estimation)

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Atomic model buiding 1

RefinementProtocol: OTHER

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