Elongation factor Tu: a regulatory GTPase with an integrated effector
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Affinity Precipitation of Active Rho-GEFs Using a GST-tagged Mutant Rho Protein (GST-RhoA(G17A)) from Epithelial Cell Lysates
Published on: March 31, 2012
1Laboratorium für Biochemie, Universität Bayreuth, Germany.
Abstract:
Several elongation factors involved in protein synthesis are GTPases that share structural and mechanistic homology with the large family of proteins including Ras and heterotrimeric receptor-coupled G proteins. The structure of elongation factor Tu (EF-Tu) from thermophilic bacteria, in its 'active' GTP-bound form, has recently been solved by X-ray crystallography. Comparison of this structure with the structure of Escherichia coli EF-Tu bound to GDP reveals a dramatic conformational change that is dependent on GTPase activity. The mechanism of this conformational change and of GTPase activation are discussed, and a model for the EF-Tu-GTP complex with aminoacyl-tRNA is presented.
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