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Structural Basis for mRNA and tRNA Positioning on the Ribosome
Veysel Berk, Wen Zhang, Raj D. Pai and Jamie H. Doudna Cate
Proceedings of the National Academy of Sciences of the United States of America
Vol. 103, No. 43 (Oct. 24, 2006), pp. 15830-15834
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/30052065
Page Count: 5
You can always find the topics here!Topics: Messenger RNA, Ribosomes, Nucleotides, Transfer RNA, Electron density, Phosphates, Proteins, Anticodon, Crystals, Crystal structure
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Protein synthesis requires the accurate positioning of mRNA and tRNA in the peptidyl-tRNA site of the ribosome. Here we describe x-ray crystal structures of the intact bacterial ribosome from Escherichia coli in a complex with mRNA and the anticodon stem-loop of P-site tRNA. At 3.5-Å resolution, these structures reveal rearrangements in the intact ribosome that clamp P-site tRNA and mRNA on the small ribosomal subunit. Binding of the anticodon stem-loop of P-site tRNA to the ribosome is sufficient to lock the head of the small ribosomal subunit in a single conformation, thereby preventing movement of mRNA and tRNA before mRNA decoding.
Proceedings of the National Academy of Sciences of the United States of America © 2006 National Academy of Sciences