Abstract
The crystal structure of the EF-Tu.EF-Ts complex from Escherichia coli has been determined to a resolution of 2.5 A. The complex contains two subunits of each of the elongation factors. The two EF-Ts molecules form a tight dimer, but there is little contact between the two EF-Tu molecules. The interaction of EF-Ts with EF-Tu results principally in the disruption of the Mg2+ ion binding site, thereby reducing the affinity of EF-Tu for guanine nucleotides.
MeSH terms
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Amino Acid Sequence
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Crystallography, X-Ray
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Escherichia coli / chemistry*
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Guanosine Diphosphate / chemistry
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Magnesium / chemistry
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Models, Molecular
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Molecular Sequence Data
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Peptide Elongation Factor Tu / chemistry*
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Peptide Elongation Factors / chemistry*
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Protein Binding
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Protein Conformation
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Protein Structure, Secondary
Substances
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Peptide Elongation Factors
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elongation factor Ts
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Guanosine Diphosphate
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Peptide Elongation Factor Tu
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Magnesium