Abstract
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-A 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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Base Sequence
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Crystallography, X-Ray
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Escherichia coli / chemistry
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Models, Molecular
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Nucleic Acid Conformation
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Protein Binding
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RNA, Messenger / chemistry
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RNA, Messenger / genetics
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RNA, Messenger / metabolism
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RNA, Transfer / chemistry*
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RNA, Transfer / genetics
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RNA, Transfer / metabolism*
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Ribosomal Proteins / chemistry
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Ribosomal Proteins / metabolism
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Ribosomes / chemistry
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Ribosomes / genetics*
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Ribosomes / metabolism*
Substances
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RNA, Messenger
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Ribosomal Proteins
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RNA, Transfer
Associated data
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PDB/2I2P
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PDB/2I2T
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PDB/2I2U
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PDB/2I2V