Crystal structure of Thermatoga mritima ribosome recycling factor: A tRNA mimic

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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 β/α/β 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.

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  • Biological Sciences
Original languageEnglish
Pages (from-to)2349-2352
JournalScience
Volume286
Issue number5448
Publication statusPublished - 1999
Publication categoryResearch
Peer-reviewedYes