4W29

70S ribosome translocation intermediate containing elongation factor EFG/GDP/fusidic acid, mRNA, and tRNAs trapped in the AP/AP pe/E chimeric hybrid state.

This is a non-PDB format compatible entry.

Summary for 4W29

• Entry DOI: 10.2210/pdb4w29/pdb
• Descriptor: 30S ribosomal protein S2, 30S ribosomal protein S11, 30S ribosomal protein S12, ... (64 entities in total)
• Functional Keywords: chimeric hybrid state ribosome, translocation intermediate, ef-g, mrna, trna, ribosome-antibiotic complex, ribosome/antibiotic
• Biological source: Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039); More
• Cellular location: Cytoplasm : Q72I01
• Total number of polymer chains: 122
• Total formula weight: 4630819.49

Authors

Zhou, J.,Lancaster, L.,Donohue, J.P.,Noller, H.F. (deposition date: 2014-07-02, release date: 2014-10-01, Last modification date: 2023-09-20)

Primary citation

Zhou, J.,Lancaster, L.,Donohue, J.P.,Noller, H.F.
How the ribosome hands the A-site tRNA to the P site during EF-G-catalyzed translocation.
Science, 345:1188-1191, 2014

PubMed Abstract: Coupled translocation of messenger RNA and transfer RNA (tRNA) through the ribosome, a process catalyzed by elongation factor EF-G, is a crucial step in protein synthesis. The crystal structure of a bacterial translocation complex describes the binding states of two tRNAs trapped in mid-translocation. The deacylated P-site tRNA has moved into a partly translocated pe/E chimeric hybrid state. The anticodon stem-loop of the A-site tRNA is captured in transition toward the 30S P site, while its 3' acceptor end contacts both the A and P loops of the 50S subunit, forming an ap/ap chimeric hybrid state. The structure shows how features of ribosomal RNA rearrange to hand off the A-site tRNA to the P site, revealing an active role for ribosomal RNA in the translocation process.

PubMed: 25190797
DOI: 10.1126/science.1255030

Experimental method

X-RAY DIFFRACTION (3.8 Å)