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The structure of the Escherichia coli EF-Tu· EF-Ts complex at 2.5 Å resolution

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A Correction to this article was published on 09 May 1996

Abstract

The crystal structure of the EF-Tu·EF-Ts complex from Escherichia coli has been determined to a resolution of 2.5 Å. The complex contains two subunits of each of the elongation factors. The two EF-Ts molecules form a tight dirtier, 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.

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Authors and Affiliations

  1. European Molecular Biology Laboratory, Grenoble Outstation, B.P. 156, 38042, Grenoble Cedex, France

    Takemasa Kawashima, Carmen Berthet-Colominas, Stephen Cusack & Reuben Leberman

  2. European Synchrotron Radiation Facility, B.P. 220, 38043, Grenoble Cedex, France

    Michael Wulff

Authors
  1. Takemasa Kawashima
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  2. Carmen Berthet-Colominas
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  3. Michael Wulff
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  4. Stephen Cusack
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  5. Reuben Leberman
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Kawashima, T., Berthet-Colominas, C., Wulff, M. et al. The structure of the Escherichia coli EF-Tu· EF-Ts complex at 2.5 Å resolution. Nature 379, 511–518 (1996). https://doi.org/10.1038/379511a0

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