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.