EMD-29730

Single-particle
3.14 Å
EMD-29730 Deposition: 10/02/2023
Map released: 31/01/2024
Last modified: 23/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-29730

40S ribosomal subunit of the 80S Giardia intestinalis assemblage A ribosome with Emetine bound in V2 conformation with mRNA and three tRNAs.

EMD-29730

Single-particle
3.14 Å
EMD-29730 Deposition: 10/02/2023
Map released: 31/01/2024
Last modified: 23/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Giardia intestinalis assemblage A
Sample: 40S ribosomal subunit of the 80S Giardia intestinalis assemblage A ribosome with Emetine bound in V1 conformation
Fitted models: 8g4s (Avg. Q-score: 0.51)

Deposition Authors: Eiler DR, Wimberly BT, Bilodeau DY, Rissland OS, Kieft JS
The Giardia lamblia ribosome structure reveals divergence in several biological pathways and the mode of emetine function.
PUBMED: 38242118
DOI: doi:10.1016/j.str.2023.12.015
ISSN: 0969-2126
ASTM: STRUE6
Abstract:
Giardia lamblia is a deeply branching protist and a human pathogen. Its unusual biology presents the opportunity to explore conserved and fundamental molecular mechanisms. We determined the structure of the G. lamblia 80S ribosome bound to tRNA, mRNA, and the antibiotic emetine by cryo-electron microscopy, to an overall resolution of 2.49 Å. The structure reveals rapidly evolving protein and nucleotide regions, differences in the peptide exit tunnel, and likely altered ribosome quality control pathways. Examination of translation initiation factor binding sites suggests these interactions are conserved despite a divergent initiation mechanism. Highlighting the potential of G. lamblia to resolve conserved biological principles; our structure reveals the interactions of the translation inhibitor emetine with the ribosome and mRNA, thus providing insight into the mechanism of action for this widely used antibiotic. Our work defines key questions in G. lamblia and motivates future experiments to explore the diversity of eukaryotic gene regulation.