doi: 10.1038/379511a0.
The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution
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- PMID: 8596629
- DOI: 10.1038/379511a0
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The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution
Nature.
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Erratum in
- Nature 1996 May 9;381(6578):172
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.
Comment in
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Protein synthesis. An elongation factor turn-on.Nature. 1996 Feb 8;379(6565):491-2. doi: 10.1038/379491a0. Nature. 1996. PMID: 8596624 No abstract available.
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