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. 1993 Sep 9;365(6442):126-32.
doi: 10.1038/365126a0.

Crystal structure of active elongation factor Tu reveals major domain rearrangements

H Berchtold  1 , L Reshetnikova, C O Reiser, N K Schirmer, M Sprinzl, R Hilgenfeld
Affiliations

Crystal structure of active elongation factor Tu reveals major domain rearrangements

H Berchtold et al. Nature. .

Erratum in

  • Nature 1993 Sep 23;365(6444):368

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 A, with incorporation of data extending to 1.45 A. The effector region, including interaction sites for the ribosome and for transfer RNA, is well defined. Molecular mechanisms are proposed for transduction 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 rearrangements of the three domains of the molecule.

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