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Crystal Structure of Thermotoga maritima Ribosome Recycling Factor: A tRNA Mimic

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Science  17 Dec 1999:
Vol. 286, Issue 5448, pp. 2349-2352
DOI: 10.1126/science.286.5448.2349

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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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