Ribosomal Protein S7 from
Bacillus stearothermophilus and Pyrococcus horikoshii

[Ribosomal Protein S7]

left: B. Stearothermophilus            right: P. horikoshii   

Ribosomal protein S7 is located at the head of the small subunit facing to the decoding center. It is one of the primary 16S rRNA binding proteins responsible for initiating the assembly of the head of the 30S subunit. It is also the major protein component cross-linked with tRNA molecules bound at both A and P sites.
The structure of ribosomal protein S7 from Bacillus stearothermophilus and Pyrococcus horikoshii has been solved by the multiwavelength anomalous diffraction method using Se-Met substituted proteins. The molecule consists of a helical hydrophobic core domain and a beta-ribbon arm extending from the hydrophobic core. The helical core domain is composed of a pair of entangled helix-turn-helix motifs similar to 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 feature, together with former cross-link experiments, suggests how S7 binds to the 3' major domain of 16S rRNA and mediates the folding of 16S rRNA to create the ribosome decoding center.

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