Abstract
Cryo-EM density maps showing the 70S ribosome of E. coli in two different functional states related by a ratchet-like motion were analyzed using real-space refinement. Comparison of the two resulting atomic models shows that the ribosome changes from a compact structure to a looser one, coupled with the rearrangement of many of the proteins. Furthermore, in contrast to the unchanged inter-subunit bridges formed wholly by RNA, the bridges involving proteins undergo large conformational changes following the ratchet-like motion, suggesting an important role of ribosomal proteins in facilitating the dynamics of translation.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Bacterial Proteins / chemistry*
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Bacterial Proteins / ultrastructure
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Escherichia coli / genetics*
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Escherichia coli / metabolism*
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Macromolecular Substances
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Models, Molecular
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Molecular Conformation
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Molecular Weight
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Protein Biosynthesis / physiology
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Protein Structure, Quaternary / physiology*
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Protein Structure, Tertiary / physiology
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RNA / chemistry*
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Ribosomal Proteins / chemistry*
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Ribosomal Proteins / ultrastructure
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Ribosomes / chemistry*
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Ribosomes / ultrastructure
Substances
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Bacterial Proteins
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Macromolecular Substances
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Ribosomal Proteins
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RNA
Associated data
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PDB/1P6G
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PDB/1P85
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PDB/1P86
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PDB/1P87