4WQU

Crystal structure of the Thermus thermophilus 70S ribosome in complex with elongation factor G trapped by the antibiotic dityromycin

This is a non-PDB format compatible entry.

Summary for 4WQU

• Entry DOI: 10.2210/pdb4wqu/pdb
• Related: 4WPO 4WQF 4WQY
• Related PRD ID: PRD_001218
• Descriptor: 23S Ribosomal RNA, 50S ribosomal protein L11, 50S ribosomal protein L13, ... (63 entities in total)
• Functional Keywords: ribosome, efg, elongation, translocation, ribosome-antibiotic complex, ribosome/antibiotic
• Biological source: Escherichia coli str. K-12 substr. MC4100; More
• Total number of polymer chains: 118
• Total formula weight: 4754767.55

Authors

Lin, J.,Gagnon, M.G.,Steitz, T.A. (deposition date: 2014-10-22, release date: 2015-01-28, Last modification date: 2024-12-25)

Primary citation

Lin, J.,Gagnon, M.G.,Bulkley, D.,Steitz, T.A.
Conformational Changes of Elongation Factor G on the Ribosome during tRNA Translocation.
Cell, 160:219-227, 2015

PubMed Abstract: The universally conserved GTPase elongation factor G (EF-G) catalyzes the translocation of tRNA and mRNA on the ribosome after peptide bond formation. Despite numerous studies suggesting that EF-G undergoes extensive conformational rearrangements during translocation, high-resolution structures exist for essentially only one conformation of EF-G in complex with the ribosome. Here, we report four atomic-resolution crystal structures of EF-G bound to the ribosome programmed in the pre- and posttranslocational states and to the ribosome trapped by the antibiotic dityromycin. We observe a previously unseen conformation of EF-G in the pretranslocation complex, which is independently captured by dityromycin on the ribosome. Our structures provide insights into the conformational space that EF-G samples on the ribosome and reveal that tRNA translocation on the ribosome is facilitated by a structural transition of EF-G from a compact to an elongated conformation, which can be prevented by the antibiotic dityromycin.

PubMed: 25594181
DOI: 10.1016/j.cell.2014.11.049

Experimental method

X-RAY DIFFRACTION (2.8 Å)