Abstract
Bacterial release factor RF2 promotes termination of protein synthesis, specifically recognizing stop codons UAA or UGA. The crystal structure of Escherichia coli RF2 has been determined to a resolution of 1.8 A. RF2 is structurally distinct from its eukaryotic counterpart eRF1. The tripeptide SPF motif, thought to confer RF2 stop codon specificity, and the universally conserved GGQ motif, proposed to be involved with the peptidyl transferase center, are exposed in loops only 23 A apart, and the structure suggests that stop signal recognition is more complex than generally believed.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Conserved Sequence
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Crystallization
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Crystallography, X-Ray
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Escherichia coli Proteins*
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Humans
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Models, Molecular
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Molecular Mimicry
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Molecular Sequence Data
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Nucleic Acid Conformation
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Peptide Termination Factors / chemistry*
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Peptide Termination Factors / metabolism
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Protein Structure, Secondary
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Protein Structure, Tertiary
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RNA, Transfer / chemistry
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RNA, Transfer / genetics
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RNA, Transfer / metabolism
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Sequence Alignment
Substances
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ETF1 protein, human
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Escherichia coli Proteins
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Peptide Termination Factors
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peptide chain termination release factor 2
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prfB protein, E coli
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RNA, Transfer