Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacteria / chemistry*
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / isolation & purification
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Base Sequence
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Binding Sites
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Cloning, Molecular
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Crystallography, X-Ray
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DNA Primers
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Nucleic Acid Conformation
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Peptide Elongation Factors / chemistry*
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Peptide Elongation Factors / genetics
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Peptide Elongation Factors / isolation & purification
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Peptide Fragments / chemistry
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Peptide Fragments / isolation & purification
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RNA, Messenger / chemistry
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RNA, Messenger / genetics
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Recombinant Proteins / chemistry
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Recombinant Proteins / isolation & purification
Substances
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Bacterial Proteins
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DNA Primers
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Peptide Elongation Factors
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Peptide Fragments
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RNA, Messenger
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Recombinant Proteins
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SelB protein, Bacteria