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Role of the conserved aspartate and phenylalanine residues in prokaryotic and mitochondrial elongation factor Ts in guanine nucleotide exchange.

作者信息

Zhang Y, Li X, Spremulli L L

机构信息

Department of Chemistry, University of North Carolina, Chapel Hill 27599-3290, USA.

出版信息

FEBS Lett. 1996 Aug 12;391(3):330-2. doi: 10.1016/0014-5793(96)00789-2.

DOI:10.1016/0014-5793(96)00789-2
PMID:8765000
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.

摘要

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