A ribosomal protein module in EF-G and DNA gyrase.
A novel common fold observed in the structures of elongation factor G, DNA gyrase B, and ribosomal protein S5 displays a rare topological feature suggesting the high probability of an evolutionary relationship.
Murzin
A G
AG
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D005075:Biological Evolution; D027081:DNA Gyrase; D004250:DNA Topoisomerases, Type II / Q000737:chemistry*; D004926:Escherichia coli / Q000201:enzymology; D001411:Geobacillus stearothermophilus / Q000201:enzymology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D012269:Ribosomal Proteins / Q000737:chemistry*; D016963:Thermus thermophilus / Q000201:enzymology
D001426:Bacterial Proteins; D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors; D012269:Ribosomal Proteins; C030831:ribosomal protein S5; D027081:DNA Gyrase; D004250:DNA Topoisomerases, Type II