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

E-ISSN： 1744-3091|61|3|296-298

ISSN： 1744-3091

Source： Acta Crystallographica Section F, Vol.61, Iss.3, 2005-03, pp. : 296-298

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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‐tRNA^Sec) 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 P2₁2₁2, with unit‐cell parameters a = 81.69, b = 169.58, c = 71.69 Å.