title: Elongation factor Tu: a regulatory GTPase with an integrated effector.
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.
authors.affiliation: Laboratorium für Biochemie, Universität Bayreuth, Germany.
authors.forename: M
authors.initials: M
authors.lastname: Sprinzl
mesh_terms: D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000737:chemistry / Q000201:enzymology; D020963:GTP Phosphohydrolase-Linked Elongation Factors / Q000737:chemistry*; D006153:Guanosine Diphosphate / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D008969:Molecular Sequence Data; D010444:Peptide Elongation Factor Tu / Q000737:chemistry*; D011487:Protein Conformation; D016963:Thermus thermophilus / Q000737:chemistry / Q000201:enzymology
chemical_list: D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate; D020963:GTP Phosphohydrolase-Linked Elongation Factors; D010444:Peptide Elongation Factor Tu