5OT7

Elongation factor G-ribosome complex captures in the absence of inhibitors.

This is a non-PDB format compatible entry.

Summary for 5OT7

• Entry DOI: 10.2210/pdb5ot7/pdb
• EMDB information: 3852
• Descriptor: 16S Ribosomal RNA, 30S ribosomal protein S4, 30S ribosomal protein S5, ... (62 entities in total)
• Functional Keywords: elongation factor g, translation, translocation, ribosome
• Biological source: Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579); More
• Cellular location: Cytoplasm: Q5SHN5
• Total number of polymer chains: 59
• Total formula weight: 2303759.09

Authors

Mace, K.,Giudice, E.,Chat, S.,Gillet, R. (deposition date: 2017-08-21, release date: 2018-02-14, Last modification date: 2018-04-11)

Primary citation

Mace, K.,Giudice, E.,Chat, S.,Gillet, R.
The structure of an elongation factor G-ribosome complex captured in the absence of inhibitors.
Nucleic Acids Res., 46:3211-3217, 2018

PubMed Abstract: During translation's elongation cycle, elongation factor G (EF-G) promotes messenger and transfer RNA translocation through the ribosome. Until now, the structures reported for EF-G-ribosome complexes have been obtained by trapping EF-G in the ribosome. These results were based on use of non-hydrolyzable guanosine 5'-triphosphate (GTP) analogs, specific inhibitors or a mutated EF-G form. Here, we present the first cryo-electron microscopy structure of EF-G bound to ribosome in the absence of an inhibitor. The structure reveals a natural conformation of EF-G·GDP in the ribosome, with a previously unseen conformation of its third domain. These data show how EF-G must affect translocation, and suggest the molecular mechanism by which fusidic acid antibiotic prevents the release of EF-G after GTP hydrolysis.

PubMed: 29408956
DOI: 10.1093/nar/gky081

Experimental method

ELECTRON MICROSCOPY (3.8 Å)