3J7Z

Structure of the E. coli 50S subunit with ErmCL nascent chain

Summary for 3J7Z

• Entry DOI: 10.2210/pdb3j7z/pdb
• EMDB information: 6057
• Descriptor: 50S ribosomal protein L32, 5S rRNA, 50S ribosomal protein L2, ... (36 entities in total)
• Functional Keywords: erythromycin, stalling, ribosome-antibiotic complex, ribosome/antibiotic
• Biological source: Escherichia coli K-12; More
• Total number of polymer chains: 35
• Total formula weight: 1390525.36

Authors

Arenz, S.,Meydan, S.,Starosta, A.L.,Berninghausen, O.,Beckmann, R.,Vazquez-Laslop, N.,Wilson, D.N. (deposition date: 2014-08-27, release date: 2014-10-22, Last modification date: 2018-07-18)

Primary citation

Arenz, S.,Meydan, S.,Starosta, A.L.,Berninghausen, O.,Beckmann, R.,Vazquez-Laslop, N.,Wilson, D.N.
Drug Sensing by the Ribosome Induces Translational Arrest via Active Site Perturbation.
Mol.Cell, 56:446-452, 2014

PubMed Abstract: During protein synthesis, nascent polypeptide chains within the ribosomal tunnel can act in cis to induce ribosome stalling and regulate expression of downstream genes. The Staphylococcus aureus ErmCL leader peptide induces stalling in the presence of clinically important macrolide antibiotics, such as erythromycin, leading to the induction of the downstream macrolide resistance methyltransferase ErmC. Here, we present a cryo-electron microscopy (EM) structure of the erythromycin-dependent ErmCL-stalled ribosome at 3.9 Å resolution. The structure reveals how the ErmCL nascent chain directly senses the presence of the tunnel-bound drug and thereby induces allosteric conformational rearrangements at the peptidyltransferase center (PTC) of the ribosome. ErmCL-induced perturbations of the PTC prevent stable binding and accommodation of the aminoacyl-tRNA at the A-site, leading to inhibition of peptide bond formation and translation arrest.

PubMed: 25306253
DOI: 10.1016/j.molcel.2014.09.014

Experimental method

ELECTRON MICROSCOPY (3.9 Å)