Abstract
Cryo-EM analysis of a wild-type Escherichia coli pretranslocational sample has revealed the presence of previously unseen intermediate substates of the bacterial ribosome during the first phase of translocation, characterized by intermediate intersubunit rotations, L1 stalk positions, and tRNA configurations. Furthermore, we describe the domain rearrangements in quantitative terms, which has allowed us to characterize the processivity and coordination of the conformational reorganization of the ribosome, along with the associated changes in tRNA ribosome-binding configuration. The results are consistent with the view of the ribosome as a molecular machine employing Brownian motion to reach a functionally productive state via a series of substates with incremental changes in conformation.
Publication types
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Research Support, N.I.H., Extramural
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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.
MeSH terms
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Binding Sites
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Cryoelectron Microscopy
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Crystallography, X-Ray
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Macromolecular Substances / chemistry
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Macromolecular Substances / ultrastructure
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Models, Molecular
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Molecular Conformation
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Protein Biosynthesis*
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RNA, Messenger / genetics
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RNA, Messenger / metabolism*
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RNA, Messenger / ultrastructure
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RNA, Transfer / genetics
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RNA, Transfer / metabolism*
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RNA, Transfer / ultrastructure
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Ribosomes / metabolism*
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Ribosomes / ultrastructure
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Thermodynamics
Substances
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Macromolecular Substances
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RNA, Messenger
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RNA, Transfer
Associated data
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PDB/3J0T
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PDB/3J0U
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PDB/3J0V
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PDB/3J0W
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PDB/3J0X
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PDB/3J0Y
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PDB/3J0Z
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PDB/3J10
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PDB/3J11
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PDB/3J12
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PDB/3J13
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PDB/3J14