Crystallization and preliminary X-ray analysis of the mRNA-binding domain of elongation factor SelB in complex with RNA

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

    Research output: Contribution to journalArticlepeer-review

    3 Citations (Scopus)

    Abstract

    In bacteria, the selenocysteine-specific elongation factor SelB is necessary for incorporation of selenocysteine, the 21st amino acid, into proteins by the ribosome. SelB binds to an mRNA hairpin formed by the selenocysteine-insertion sequence (SECIS) and delivers selenocysteyl-tRNA (Sec-tRNASec) at the ribosomal A site. The minimum fragment (residues 512-634) of Moorella thermoacetica SelB (SelB-M) required for mRNA binding has been overexpressed and purified. The complex of SelB-M with 23 nucleotides of the SECIS mRNA hairpin was crystallized at 293 K using the hanging-drop vapour-diffusion or oil-batch methods. The crystals diffract to 2.3 Å resolution using SPring-8 BL41XU and belong to the space group P2 1212, with unit-cell parameters a = 81.69, b = 169.58, c = 71.69 Å.

    Original languageEnglish
    Pages (from-to)296-298
    Number of pages3
    JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
    Volume61
    Issue number3
    DOIs
    Publication statusPublished - 2005

    All Science Journal Classification (ASJC) codes

    • Biophysics
    • Structural Biology
    • Biochemistry
    • Genetics
    • Condensed Matter Physics

    Fingerprint Dive into the research topics of 'Crystallization and preliminary X-ray analysis of the mRNA-binding domain of elongation factor SelB in complex with RNA'. Together they form a unique fingerprint.

    Cite this