Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1.
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.
Vestergaard
B
B
Institute of Molecular and Structural Biology, University of Aarhus, DK-8000 Aarhus C, Denmark.
Van
L B
LB
Andersen
G R
GR
Nyborg
J
J
Buckingham
R H
RH
Kjeldgaard
M
M
D000595:Amino Acid Sequence; D017124:Conserved Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D029968:Escherichia coli Proteins; D006801:Humans; D008958:Models, Molecular; D018716:Molecular Mimicry; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D010454:Peptide Termination Factors / Q000737:chemistry* / Q000378:metabolism; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012343:RNA, Transfer / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment
C489002:ETF1 protein, human; D029968:Escherichia coli Proteins; D010454:Peptide Termination Factors; C041460:peptide chain termination release factor 2; C489006:prfB protein, E coli; D012343:RNA, Transfer