4V5M

tRNA tranlocation on the 70S ribosome: the pre-translocational translocation intermediate TI(PRE)

This is a non-PDB format compatible entry.

Summary for 4V5M

• Entry DOI: 10.2210/pdb4v5m/pdb
• Related: 1DAR 1DV4 1EFG 1EG0 1ELO 1EMI 1FJG 1FKA 1G1X 1GIX 1HNW 1HNX 1HNZ 1HR0 1I94 1I95 1I96 1I97 1IBK 1IBL 1IBM 1J5E 1JGO 1JGP 1JGQ 1L1U 1N32 1N33 1N34 1N36 1PN7 1PN8 1PNS 1PNX 1QD7 1QZC 1RSS 1TWT 1VOV 1XMO 1XMQ 1XNQ 1XNR 1YL4 2B64 2B9M 2B9O 2EFG 2F4V 2J00 2J02 2JL5 2JL7 2UU9 2UUA 2UUB 2UUC 2UXB 2UXC 2UXD 2V46 2V48 2VQE 2VQF 2WDG 2WDH 2WDK 2WDM 2WH1 2WH3 2WRN 2WRQ 2X9R 2X9T 2XFZ 2XG1 2XQD
• EMDB information: 1798
• Descriptor: 16S RRNA, 30S RIBOSOMAL PROTEIN S10, 30S RIBOSOMAL PROTEIN S11, ... (59 entities in total)
• Functional Keywords: ribosome, translation, elongation cycle
• Biological source: THERMUS THERMOPHILUS; More
• Total number of polymer chains: 57
• Total formula weight: 2311295.79

Authors

Ratje, A.H.,Loerke, J.,Mikolajka, A.,Bruenner, M.,Hildebrand, P.W.,Starosta, A.L.,Doenhoefer, A.,Connell, S.R.,Fucini, P.,Mielke, T.,Whitford, P.C.,Onuchic, J.N.,Yu, Y.,Sanbonmatsu, K.Y.,Hartmann, R.K.,Penczek, P.A.,Wilson, D.N.,Spahn, C.M.T. (deposition date: 2010-10-01, release date: 2014-07-09, Last modification date: 2019-12-11)

Primary citation

Ratje, A.H.,Loerke, J.,Mikolajka, A.,Brunner, M.,Hildebrand, P.W.,Starosta, A.L.,Donhofer, A.,Connell, S.R.,Fucini, P.,Mielke, T.,Whitford, P.C.,Onuchic, J.N.,Yu, Y.,Sanbonmatsu, K.Y.,Hartmann, R.K.,Penczek, P.A.,Wilson, D.N.,Spahn, C.M.T.
Head Swivel on the Ribosome Facilitates Translocation by Means of Intra-Subunit tRNA Hybrid Sites.
Nature, 468:713-, 2010

PubMed Abstract: The elongation cycle of protein synthesis involves the delivery of aminoacyl-transfer RNAs to the aminoacyl-tRNA-binding site (A site) of the ribosome, followed by peptide-bond formation and translocation of the tRNAs through the ribosome to reopen the A site. The translocation reaction is catalysed by elongation factor G (EF-G) in a GTP-dependent manner. Despite the availability of structures of various EF-G-ribosome complexes, the precise mechanism by which tRNAs move through the ribosome still remains unclear. Here we use multiparticle cryoelectron microscopy analysis to resolve two previously unseen subpopulations within Thermus thermophilus EF-G-ribosome complexes at subnanometre resolution, one of them with a partly translocated tRNA. Comparison of these substates reveals that translocation of tRNA on the 30S subunit parallels the swivelling of the 30S head and is coupled to unratcheting of the 30S body. Because the tRNA maintains contact with the peptidyl-tRNA-binding site (P site) on the 30S head and simultaneously establishes interaction with the exit site (E site) on the 30S platform, a novel intra-subunit 'pe/E' hybrid state is formed. This state is stabilized by domain IV of EF-G, which interacts with the swivelled 30S-head conformation. These findings provide direct structural and mechanistic insight into the 'missing link' in terms of tRNA intermediates involved in the universally conserved translocation process.

PubMed: 21124459
DOI: 10.1038/NATURE09547

Experimental method

ELECTRON MICROSCOPY (7.8 Å)