title: Role of the conserved aspartate and phenylalanine residues in prokaryotic and mitochondrial elongation factor Ts in guanine nucleotide exchange.
abstract: The guanine nucleotide exchange reaction catalyzed by elongation factor Ts is proposed to arise from the intrusion of the side chains of D80 and F81 near the Mg2+ binding site in EF-Tu. D80A and F81A mutants of E. coli EF-Ts were 2-3-fold less active in promoting GDP exchange with E. coli EF-Tu while the D80AF81A mutant was nearly 10-fold less active. The D84 and F85 mutants of EF-Tsmt were 5-10-fold less active in stimulating the activity of EF-Tumt. The double mutation completely abolished the activity of EF-Tsmt.
authors.affiliation: Department of Chemistry, University of North Carolina, Chapel Hill 27599-3290, USA.
authors.forename: Y
authors.initials: Y
authors.lastname: Zhang
authors.forename: X
authors.initials: X
authors.lastname: Li
authors.forename: L L
authors.initials: LL
authors.lastname: Spremulli
mesh_terms: D001224:Aspartic Acid / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli; D006150:Guanine Nucleotides / Q000378:metabolism*; D006153:Guanosine Diphosphate / Q000378:metabolism; D010445:Peptide Elongation Factors / Q000378:metabolism*; D010649:Phenylalanine / Q000378:metabolism*; D011072:Poly U / Q000378:metabolism; D013329:Structure-Activity Relationship
chemical_list: D006150:Guanine Nucleotides; D010445:Peptide Elongation Factors; C023512:elongation factor Ts; D006153:Guanosine Diphosphate; D011072:Poly U; D001224:Aspartic Acid; D010649:Phenylalanine