Sequential resonance assignments as a basis for the determination of a three-dimensional structure of protein E-L30 of Escherichia coli.
Nuclear Overhauser enhancement spectra of ribosomal protein E-L30 were searched for interresidual connectivities involving peptide bond amide protons in order to establish sequential neighbourships between amino acid residues. By comparing these data with the actual amino acid sequence of the protein, sequential resonance assignments became available for almost 90% for the amino acids in E-L30. With the aid of these assignments, some 30 nuclear Overhauser connectivities could be interpreted in terms of short interproton distances involving remote sites in the polypeptide chain. It turned out that these contacts between residues generated enough constraints to permit construction of a three-dimensional structure for the protein.
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D004926:Escherichia coli / Q000032:analysis*; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D011522:Protons; D012269:Ribosomal Proteins
D001426:Bacterial Proteins; D046911:Macromolecular Substances; D011522:Protons; D012269:Ribosomal Proteins; C035201:ribosomal protein L30