Crystal structure of the transfer-RNA domain of transfer-messenger RNA in complex with SmpB

Sascha Gutmann, Peter W. Haebel, Laurent Metzinger, Markus Sutter, Brice Felden and Nenad Ban ()
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Sascha Gutmann: Eidgenössische Technische Hochschule Hönggerberg (ETH Zürich)
Peter W. Haebel: Eidgenössische Technische Hochschule Hönggerberg (ETH Zürich)
Laurent Metzinger: Biochimie Pharmaceutique UPRES JE2311, Université de Rennes I
Markus Sutter: Eidgenössische Technische Hochschule Hönggerberg (ETH Zürich)
Brice Felden: Biochimie Pharmaceutique UPRES JE2311, Université de Rennes I
Nenad Ban: Eidgenössische Technische Hochschule Hönggerberg (ETH Zürich)

Nature, 2003, vol. 424, issue 6949, 699-703

Abstract: Abstract Accurate translation of genetic information into protein sequence depends on complete messenger RNA molecules. Truncated mRNAs cause synthesis of defective proteins, and arrest ribosomes at the end of their incomplete message. In bacteria, a hybrid RNA molecule that combines the functions of both transfer and messenger RNAs (called tmRNA) rescues stalled ribosomes, and targets aberrant, partially synthesized, proteins for proteolytic degradation1,2. Here we report the 3.2-Å-resolution structure of the tRNA-like domain of tmRNA (tmRNAΔ) in complex with small protein B (SmpB), a protein essential for biological functions of tmRNA. We find that the flexible RNA molecule adopts an open L-shaped conformation and SmpB binds to its elbow region, stabilizing the single-stranded D-loop in an extended conformation. The most striking feature of the structure of tmRNAΔ is a 90° rotation of the TΨC-arm around the helical axis. Owing to this unusual conformation, the SmpB–tmRNAΔ complex positioned into the A-site of the ribosome orients SmpB towards the small ribosomal subunit, and directs tmRNA towards the elongation-factor binding region of the ribosome. On the basis of this structure, we propose a model for the binding of tmRNA on the ribosome.

Date: 2003
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DOI: 10.1038/nature01831

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