title: Crystal structure of a prokaryotic ribosomal protein.
abstract: The structure of ribosomal protein L30 from Bacillus stearothermophilus has been solved to a resolution of 2.5 A. The molecule is somewhat elongated and contains two helices and a three-stranded, anti-parallel beta-pleated sheet. The protein fold, in which helices pack on the same side of the sheet, generates a simple helix-sheet, two-layered motif. It is possible to distinguish three hydrophobic patches on the molecular surface, and one end has six isolated arginine and lysine residues. It is proposed that these reflect sites of protein-protein and protein-RNA interaction, respectively. The protein fold is very similar to that of the only other known ribosomal protein structure, L7/L12 from Escherichia coli, and, based on this similarity, an attempt is made to align the amino acid sequences of the two proteins.
authors.forename: K S
authors.initials: KS
authors.lastname: Wilson
authors.forename: K
authors.initials: K
authors.lastname: Appelt
authors.forename: J
authors.initials: J
authors.lastname: Badger
authors.forename: I
authors.initials: I
authors.lastname: Tanaka
authors.forename: S W
authors.initials: SW
authors.lastname: White
mesh_terms: D003461:Crystallography; D001411:Geobacillus stearothermophilus; D008958:Models, Molecular; D011487:Protein Conformation; D012269:Ribosomal Proteins; D012270:Ribosomes / Q000648:ultrastructure; D012995:Solubility
chemical_list: D012269:Ribosomal Proteins