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• W2022842289 endingPage "2352" @default.
• W2022842289 startingPage "2349" @default.
• W2022842289 abstract "Ribosome recycling factor (RRF), together with elongation factor G (EF-G), catalyzes recycling of ribosomes after one round of protein synthesis. The crystal structure of RRF was determined at 2.55 angstrom resolution. The protein has an unusual fold where domain I is a long three-helix bundle and domain II is a three-layer beta/alpha/beta sandwich. The molecule superimposes almost perfectly with a transfer RNA (tRNA) except that the amino acid-binding 3' end is missing. The mimicry suggests that RRF interacts with the posttermination ribosomal complex in a similar manner to a tRNA, leading to disassembly of the complex. The structural arrangement of this mimicry is entirely different from that of other cases of less pronounced mimicry of tRNA so far described." @default.
• W2022842289 created "2016-06-24" @default.
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• W2022842289 date "1999-12-17" @default.
• W2022842289 modified "2023-10-18" @default.
• W2022842289 title "Crystal Structure of <i>Thermotoga maritima</i> Ribosome Recycling Factor: A tRNA Mimic" @default.
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• W2022842289 doi "https://doi.org/10.1126/science.286.5448.2349" @default.
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