Prediction of a novel topology in the N-terminal, 14 kDa fragment of Ada protein.
Previously determined protein structures have been analysed, in order to find folding motifs similar to that proposed by NMR spectroscopy, for the N-terminal, 14 kDa fragment of the Ada protein. The analyses reveal only limited similarities with the NMR-derived structural data and strongly suggest that this region of the Ada protein adopts a previously unobserved topology. Characteristic structural features, which arise from the inferred chain connectivity, are examined through comparisons with other structures. Using this information, the topology of the Ada protein 14 kDa fragment has been predicted in order to provide structural data not yet attainable from NMR experiments.
Swindells
M B
MB
Protein Engineering Research Institute, Osaka, Japan.
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D029968:Escherichia coli Proteins; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D008969:Molecular Sequence Data; D008970:Molecular Weight; D019853:O(6)-Methylguanine-DNA Methyltransferase; D010446:Peptide Fragments / Q000737:chemistry*; D017433:Protein Structure, Secondary; D014157:Transcription Factors
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D010446:Peptide Fragments; D014157:Transcription Factors; C045675:Ada protein, E coli; D019853:O(6)-Methylguanine-DNA Methyltransferase