Abstract
The L7/L12 protein forms a functionally important domain in the ribosome. This domain is involved in interaction with translation factors during protein biosynthesis. The tertiary and quaternary structure of the L7/L12 protein was established as a result of intensive studies in solution and in the ribosome. The conformational changes of L7/L12, the elongation factors Tu and G and other ribosomal proteins were traced by different experimental techniques. These changes occur upon interaction of the ribosome with the elongation factors and depend on GTP hydrolysis in accordance with the functional states of the ribosome.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Bacterial Proteins / chemistry
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Bacterial Proteins / metabolism
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Escherichia coli / metabolism
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Escherichia coli Proteins
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Models, Molecular
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Molecular Structure
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Peptide Elongation Factor G
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Peptide Elongation Factor Tu / metabolism
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Peptide Elongation Factors / metabolism
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Protein Conformation
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Ribosomal Proteins / chemistry*
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Ribosomal Proteins / metabolism*
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Ribosomes / metabolism
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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Peptide Elongation Factor G
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Peptide Elongation Factors
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Ribosomal Proteins
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rplL protein, E coli
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ribosomal protein L7-L12
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Peptide Elongation Factor Tu