8g4i

40S ribosomal subunit of the 80S Giardia intestinalis assemblage A ribosome with Emetine bound in V1 conformation

spinqualitylabelsall models 8g4i, resolution 3.24Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8g4i is a 10 chain structure with sequence from Giardia intestinalis assemblage A. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.24Å Ligands: MG, YAT, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RSSA_GIAIC Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits.[HAMAP-Rule:MF_03015] Publication Abstract from PubMed 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 A. 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. The Giardia lamblia ribosome structure reveals divergence in several biological pathways and the mode of emetine function.,Eiler DR, Wimberly BT, Bilodeau DY, Taliaferro JM, Reigan P, Rissland OS, Kieft JS Structure. 2024 Apr 4;32(4):400-410.e4. doi: 10.1016/j.str.2023.12.015. Epub 2024 , Jan 18. PMID:38242118 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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