TY - JOUR
T1 - Ribosomal protein S7
T2 - A new RNA-binding motif with structural similarities to a DNA architectural factor
AU - Hosaka, Harumi
AU - Nakagawa, Atsushi
AU - Tanaka, Isao
AU - Harada, Nao
AU - Sano, Kazunari
AU - Kimura, Makoto
AU - Yao, Min
AU - Wakatsuki, Soichi
N1 - Funding Information:
We thank V Stojanoff of the ESRF and A Thompson of EMBL Grenoble Outstation for their assistance during the MAD data collection on BM14 at the ESRF. We also thank AG Murzin, PR Evans and R Brimacombe for their careful reading of the manuscript and valuable comments. This work was supported by the Proposal-Based Advanced Industrial Technology R&D Program of the New Energy and Industrial Technology Development Organization (NEDO) of Japan and by a Grant-in-Aid for the Ministry of Education, Science and Culture of Japan. AN and IT are members of the TARA project of Tsukuba University, Japan.
PY - 1997/9/15
Y1 - 1997/9/15
N2 - 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-rink 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 Å resolution using multiwavelength anomalous diffraction and 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 168 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.
AB - 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-rink 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 Å resolution using multiwavelength anomalous diffraction and 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 168 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.
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U2 - 10.1016/S0969-2126(97)00270-0
DO - 10.1016/S0969-2126(97)00270-0
M3 - Article
C2 - 9331423
AN - SCOPUS:0031572233
SN - 0969-2126
VL - 5
SP - 1199
EP - 1208
JO - Structure with Folding & design
JF - Structure with Folding & design
IS - 9
ER -