MUTATIONAL AND CRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC ACTIVITY OF ELONGATION FACTOR Tu

Rolf Hilgenfeld1, Tanis Hogg1, Annett Wagner1, Veronika Hornung2, Heike Rütthard2, Mathias Sprinzl2, Jeroen Mesters1

1 Institute of Molecular Biotechnology, Department of Structural Biology and Crystallography, Beutenbergstr. 11, D-07745 Jena, Germany, e-mail: hilgenfd@imb-jena.de
2 University of Bayreuth,D-95440 Bayreuth, Germany

Keywords: elongation factor, EF-Tu, protein biosynthesis, translation

Elongation factor Tu (EF-Tu) is a regulatory GTPase [1] that undergoes major conformational rearrangements upon GTP hydrolysis. Crystal structures have been solved for both the active GTP form and the inactive GDP complex of the protein [2-7]. In spite of the available wealth of structural information, the exact mechanism of GTP hydrolysis, both by the isolated EF-Tu and when bound to the ribosome, remains unclear [8]. Results will be presented from an investigation into this problem, combining site-directed mutagenesis, X-ray crystallography, and molecular dynamics simulations.

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