リボソームタンパク質S7のX線結晶構造解析 X-ray Crystal Structure Analysis of Ribosomal Protein S7
The structure of ribosomal protein S7 from <I>Bacillus stearothermophilus</I> has been solved at 2.5 Å resolution by multiwavelength anomalous diffraction method using selenomethionyl-substituted proteins. The molecule consists of a helical hydrophobic core domain and a β-ribbon arm extending from the hydrophobic core. The helical core domain is composed of a pair of entangled helix-turn-helix motifs; the fold of the core is similar to that of a DNA architectural factor. Highly conserved basic and aromatic residues are clustered on one face of the S7 molecule and create a 16S rRNA contact surface. The molecular structure of S7, together with the results of previous cross-linking experiments, suggests how this ribosomal protein binds to the 3' major domain of 16S rRNA and mediates the folding of 16S rRNA to create the ribosome decoding center.
日本結晶学会誌 40(5), 316-321, 1998-10-28
The Crystallographic Society of Japan