1hus
From Proteopedia
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RIBOSOMAL PROTEIN S7
Overview
BACKGROUND: The ribosome is a ribonucleoprotein complex which performs the, crucial function of protein biosynthesis. Its role is to decode mRNAs, within the cell and to synthesize the corresponding proteins. Ribosomal, protein S7 is located at the head of the small (30S) subunit of the, ribosome and faces into the decoding centre. S7 is one of the primary 16S, rRNA-binding proteins responsible for initiating the assembly of the head, of the 30S subunit. In addition, S7 has been shown to be the major protein, component to cross-link with tRNA molecules bound at both the, aminoacyl-tRNA (A) and peptidyl-tRNA (P) sites of the ribosome. The, ribosomal protein S7 clearly plays an important role in ribosome function., It was hoped that an atomic-resolution structure of this protein would aid, our understanding of ribosomal mechanisms. RESULTS: The structure of, ribosomal protein S7 from Bacillus stearothermophilus has been solved at, 2.5 A resolution using multiwavelength anomalous diffraction and, selenomethionyl-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; 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. CONCLUSIONS: The molecular structure of S7, together, with the results of previous cross-linking experiments, suggest 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 centre.
About this Structure
1HUS is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.
Reference
Ribosomal protein S7: a new RNA-binding motif with structural similarities to a DNA architectural factor., Hosaka H, Nakagawa A, Tanaka I, Harada N, Sano K, Kimura M, Yao M, Wakatsuki S, Structure. 1997 Sep 15;5(9):1199-208. PMID:9331423
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