4V9M

70S Ribosome translocation intermediate FA-4.2A containing elongation factor EFG/FUSIDIC ACID/GDP, mRNA, and tRNA bound in the pe*/E state.

This is a non-PDB format compatible entry.

Summary for 4V9M

• Entry DOI: 10.2210/pdb4v9m/pdb
• Descriptor: 30S ribosomal protein S2, 30S ribosomal protein S11, 30S ribosomal protein S12, ... (61 entities in total)
• Functional Keywords: fusidic acid gdp, chimeric hybrid state ribosome, ribosome, translocation intermediate, ef-g, mrna, trna
• Biological source: Thermus thermophilus; More
• Cellular location: Cytoplasm : Q72I01
• Total number of polymer chains: 120
• Total formula weight: 4569124.15

Authors

Zhou, J.,Lancaster, L.,Donohue, J.P.,Noller, H.F. (deposition date: 2013-04-25, release date: 2014-07-09, Last modification date: 2024-11-06)

Primary citation

Zhou, J.,Lancaster, L.,Donohue, J.P.,Noller, H.F.
Crystal structures of EF-G-ribosome complexes trapped in intermediate states of translocation.
Science, 340:1236086-1236086, 2013

PubMed Abstract: Translocation of messenger and transfer RNA (mRNA and tRNA) through the ribosome is a crucial step in protein synthesis, whose mechanism is not yet understood. The crystal structures of three Thermus ribosome-tRNA-mRNA-EF-G complexes trapped with β,γ-imidoguanosine 5'-triphosphate (GDPNP) or fusidic acid reveal conformational changes occurring during intermediate states of translocation, including large-scale rotation of the 30S subunit head and body. In all complexes, the tRNA acceptor ends occupy the 50S subunit E site, while their anticodon stem loops move with the head of the 30S subunit to positions between the P and E sites, forming chimeric intermediate states. Two universally conserved bases of 16S ribosomal RNA that intercalate between bases of the mRNA may act as "pawls" of a translocational ratchet. These findings provide new insights into the molecular mechanism of ribosomal translocation.

PubMed: 23812722
DOI: 10.1126/science.1236086

Experimental method

X-RAY DIFFRACTION (4 Å)