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Crystal structure of active elongation factor Tu reveals major domain rearrangements

Nature volume 365, pages 126–132 (1993)Cite this article

An Erratum to this article was published on 23 September 1993

Abstract

The crystal structure of intact elongation factor Tu (EF-Tu) from Thermus thermophilus has been determined and refined at an effective resolution of 1.7 Å, with incorporation of data extending to 1.45 Å. The effector region, including interaction sites for the ribosome and for transfer RNA, is well defined. Molecular mechanisms are proposed for transductlon and amplification of the signal induced by GTP binding as well as for the intrinsic and effector-enhanced GTPase activity of EF-Tu. Comparison of the structure with that of EF-Tu–GDP reveals major mutual rearrange-ments of the three domains of the molecule.

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Authors and Affiliations

  1. Protein Crystallography, Central Research G 865A, Hoechst Aktiengesellschaft, D-65926, Frankfurt, Germany

    Harald Berchtold & Rolf Hilgenfeld

  2. Laboratorium für Biochemie, Universität Bayreuth, D-95440, Bayreuth, Germany

    Ludmila Reshetnikova, Christian O. A. Reiser, Norbert K. Schirmer & Mathias Sprinzl

  3. Engelhardt Institute of Molecular Biology, Russian Academy of Science, Moscow, 117984, Russia

    Ludmila Reshetnikova

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  1. Harald Berchtold
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  6. Rolf Hilgenfeld
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Berchtold, H., Reshetnikova, L., Reiser, C. et al. Crystal structure of active elongation factor Tu reveals major domain rearrangements. Nature 365, 126–132 (1993). https://doi.org/10.1038/365126a0

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