Crystal structure of elongation factor 4 bound to a clockwise ratcheted ribosome

Journal Article · Fri Aug 08 00:00:00 EDT 2014 · Science

DOI:https://doi.org/10.1126/science.1253525· OSTI ID:1354313

Gagnon, M. G.; Lin, J.; Bulkley, D.; Steitz, T. A.

Elongation factor 4 (EF4/LepA) is a highly conserved guanosine triphosphatase translation factor. It was shown to promote back-translocation of tRNAs on posttranslocational ribosome complexes and to compete with elongation factor G for interaction with pretranslocational ribosomes, inhibiting the elongation phase of protein synthesis. Here, we report a crystal structure of EF4–guanosine diphosphate bound to the Thermus thermophilus ribosome with a P-site tRNA at 2.9 angstroms resolution. The C-terminal domain of EF4 reaches into the peptidyl transferase center and interacts with the acceptor stem of the peptidyl-tRNA in the P site. The ribosome is in an unusual state of ratcheting with the 30S subunit rotated clockwise relative to the 50S subunit, resulting in a remodeled decoding center. The structure is consistent with EF4 functioning either as a back-translocase or a ribosome sequester.

• Research Organization: Brookhaven National Laboratory (BNL), Upton, NY (United States)
• Sponsoring Organization: USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
• OSTI ID: 1354313
• Report Number(s): BNL--112829-2016-JA
• Journal Information: Science, Journal Name: Science Journal Issue: 6197 Vol. 345; ISSN 0036-8075
• Publisher: AAAS
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
60 APPLIED LIFE SCIENCES