Structural basis for mRNA recognition by elongation factor SelB

Satoko Yoshizawa, Linda Rasubala, Toyoyuki Ose, Daisuke Kohda, Dominique Fourmy, Katsumi Maenaka

    Research output: Contribution to journalArticle

    58 Citations (Scopus)


    In bacteria, incorporation of selenocysteine, the 21st amino acid, into proteins requires elongation factor SelB, which has the unusual property of binding to both transfer RNA (tRNA) and mRNA. SelB binds to an mRNA hairpin formed by the selenocysteine insertion sequence (SECIS) with extremely high specificity, the molecular basis of which has been unknown. We have determined the crystal structure of the mRNA-binding domain of SelB in complex with SECIS RNA at a resolution of 2.3 Å. This is the first example of a complex between an RNA and a winged-helix (WH) domain, a motif found in many DNA-binding proteins and recently discovered in RNA-binding proteins. Notably, RNA binding does not induce a major conformational change in the WH motif. The structure reveals a new mode of RNA recognition with a geometry that allows the complex to wrap around the small ribosomal subunit.

    Original languageEnglish
    Pages (from-to)198-203
    Number of pages6
    JournalNature Structural and Molecular Biology
    Issue number2
    Publication statusPublished - Feb 20 2005

    All Science Journal Classification (ASJC) codes

    • Structural Biology
    • Molecular Biology

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