6QTZ

Cryo-EM structures of Lsg1-TAP pre-60S ribosomal particles

This is a non-PDB format compatible entry.

Summary for 6QTZ

• Entry DOI: 10.2210/pdb6qtz/pdb
• EMDB information: 10068 10071 4560 4630 4636 4884
• Descriptor: 25S rRNA, 60S ribosomal protein L13-A, 60S ribosomal protein L23-A, ... (49 entities in total)
• Functional Keywords: 60s subunit, eif6, nmd3, lsg1, ribosome
• Biological source: Saccharomyces cerevisiae; More
• Total number of polymer chains: 48
• Total formula weight: 2154021.66

Authors

Kargas, V.,Warren, A.J. (deposition date: 2019-02-26, release date: 2019-06-26, Last modification date: 2024-05-15)

Primary citation

Kargas, V.,Castro-Hartmann, P.,Escudero-Urquijo, N.,Dent, K.,Hilcenko, C.,Sailer, C.,Zisser, G.,Marques-Carvalho, M.J.,Pellegrino, S.,Wawiorka, L.,Freund, S.M.,Wagstaff, J.L.,Andreeva, A.,Faille, A.,Chen, E.,Stengel, F.,Bergler, H.,Warren, A.J.
Mechanism of completion of peptidyltransferase centre assembly in eukaryotes.
Elife, 8:-, 2019

PubMed Abstract: During their final maturation in the cytoplasm, pre-60S ribosomal particles are converted to translation-competent large ribosomal subunits. Here, we present the mechanism of peptidyltransferase centre (PTC) completion that explains how integration of the last ribosomal proteins is coupled to release of the nuclear export adaptor Nmd3. Single-particle cryo-EM reveals that eL40 recruitment stabilises helix 89 to form the uL16 binding site. The loading of uL16 unhooks helix 38 from Nmd3 to adopt its mature conformation. In turn, partial retraction of the L1 stalk is coupled to a conformational switch in Nmd3 that allows the uL16 P-site loop to fully accommodate into the PTC where it competes with Nmd3 for an overlapping binding site (base A2971). Our data reveal how the central functional site of the ribosome is sculpted and suggest how the formation of translation-competent 60S subunits is disrupted in leukaemia-associated ribosomopathies.

PubMed: 31115337
DOI: 10.7554/eLife.44904

Experimental method

ELECTRON MICROSCOPY (3.5 Å)