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Science 17 December 1999:
Vol. 286. no. 5448, pp. 2349 - 2352
DOI: 10.1126/science.286.5448.2349
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Reports

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

Maria Selmer, 1 Salam Al-Karadaghi, 1 Go Hirokawa, 2 Akira Kaji, 2 Anders Liljas 1*

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.

1 Molecular Biophysics, Center for Chemistry and Chemical Engineering, Lund University, Post Office Box 124, SE-22100 Lund, Sweden.
2 Department of Microbiology, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
*   To whom correspondence should be addressed. E-mail: anders.liljas{at}mbfys.ln.se

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