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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