7AS9

Bacillus subtilis ribosome-associated quality control complex state A. Ribosomal 50S subunit with peptidyl tRNA in the A/P position and RqcH.

Summary for 7AS9

• Entry DOI: 10.2210/pdb7as9/pdb
• EMDB information: 11890
• Descriptor: Rqc2 homolog RqcH, 50S ribosomal protein L11, 50S ribosomal protein L10, ... (32 entities in total)
• Functional Keywords: 50s, trna, rqc, rqch, peptidyl-trna, translation
• Biological source: Bacillus subtilis (strain 168); More
• Total number of polymer chains: 32
• Total formula weight: 1450947.39

Authors

Crowe-McAuliffe, C.,Wilson, D.N. (deposition date: 2020-10-27, release date: 2020-12-23, Last modification date: 2024-11-06)

Primary citation

Crowe-McAuliffe, C.,Takada, H.,Murina, V.,Polte, C.,Kasvandik, S.,Tenson, T.,Ignatova, Z.,Atkinson, G.C.,Wilson, D.N.,Hauryliuk, V.
Structural Basis for Bacterial Ribosome-Associated Quality Control by RqcH and RqcP.
Mol.Cell, 81:115-, 2021

PubMed Abstract: In all branches of life, stalled translation intermediates are recognized and processed by ribosome-associated quality control (RQC) pathways. RQC begins with the splitting of stalled ribosomes, leaving an unfinished polypeptide still attached to the large subunit. Ancient and conserved NEMF family RQC proteins target these incomplete proteins for degradation by the addition of C-terminal "tails." How such tailing can occur without the regular suite of translational components is, however, unclear. Using single-particle cryo-electron microscopy (EM) of native complexes, we show that C-terminal tailing in Bacillus subtilis is mediated by NEMF protein RqcH in concert with RqcP, an Hsp15 family protein. Our structures reveal how these factors mediate tRNA movement across the ribosomal 50S subunit to synthesize polypeptides in the absence of mRNA or the small subunit.

PubMed: 33259810
DOI: 10.1016/j.molcel.2020.11.002

Experimental method

ELECTRON MICROSCOPY (3.5 Å)