Crystal structure of active elongation factor Tu reveals major domain rearrangements

Harald Berchtold, Ludmila Reshetnikova, Christian O.A. Reiser, Norbert K. Schirmer, Mathias Sprinzl, Rolf Hilgenfeld*

*Corresponding author for this work
503 Citations (Scopus)


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.

Original languageEnglish
Issue number6442
Pages (from-to)126-132
Number of pages7
Publication statusPublished - 1993

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)


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