8G4S

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

This is a non-PDB format compatible entry.

Summary for 8G4S

• Entry DOI: 10.2210/pdb8g4s/pdb
• Related: 8FRU 8FVY 8G4I
• EMDB information: 29730
• Descriptor: 18S rRNA, 40S ribosomal protein S8, Ribosomal protein S9, ... (41 entities in total)
• Functional Keywords: giardia lamblia, ribosome structure, translation, parasite, ribosome
• Biological source: Giardia intestinalis assemblage A; More
• Total number of polymer chains: 37
• Total formula weight: 1122703.73

Authors

Eiler, D.R.,Wimberly, B.T.,Bilodeau, D.Y.,Rissland, O.S.,Kieft, J.S. (deposition date: 2023-02-10, release date: 2024-01-31, Last modification date: 2024-10-23)

Primary citation

Eiler, D.R.,Wimberly, B.T.,Bilodeau, D.Y.,Taliaferro, J.M.,Reigan, P.,Rissland, O.S.,Kieft, J.S.
The Giardia lamblia ribosome structure reveals divergence in several biological pathways and the mode of emetine function.
Structure, 32:400-, 2024

PubMed 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.

PubMed: 38242118
DOI: 10.1016/j.str.2023.12.015

Experimental method

ELECTRON MICROSCOPY (3.14 Å)