Preparation of a crystallizable mRNA-binding fragment of Moorella thermoacetica elongation factor SelB.
SelB is a bacterial elongation factor required for the decoding of a UGA stop codon together with a specific mRNA hairpin to selenocysteine. In attempts to crystallize Moorella thermoacetica SelB, a proteolysis process occurred and crystals of a proteolytic fragment were observed. The crystals, which appeared after a year, contained a C-terminal 30 kDa fragment containing the mRNA-binding domain. This fragment was reproduced through recloning. Crystals diffracting to 2.7 A were obtained.
D000595:Amino Acid Sequence; D001419:Bacteria / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D001483:Base Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D017931:DNA Primers; D009690:Nucleic Acid Conformation; D010445:Peptide Elongation Factors / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D012333:RNA, Messenger / Q000737:chemistry / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D001426:Bacterial Proteins; D017931:DNA Primers; D010445:Peptide Elongation Factors; D010446:Peptide Fragments; D012333:RNA, Messenger; D011994:Recombinant Proteins; C061878:SelB protein, Bacteria