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

2 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

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