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• W2009185547 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." @default.
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• W2009185547 date "2013-06-28" @default.
• W2009185547 modified "2023-10-12" @default.
• W2009185547 title "Crystal Structures of EF-G–Ribosome Complexes Trapped in Intermediate States of Translocation" @default.
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• W2009185547 doi "https://doi.org/10.1126/science.1236086" @default.
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