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The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution.

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.[1]

References

  1. The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution. Kawashima, T., Berthet-Colominas, C., Wulff, M., Cusack, S., Leberman, R. Nature (1996) [Pubmed]
 
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