Crystal structure of active elongation factor Tu reveals major domain rearrangements View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1993-09

AUTHORS

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

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. More... »

PAGES

126-132

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/365126a0

DOI

http://dx.doi.org/10.1038/365126a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1042485140

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8371755


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