Title : Substitution of proline 82 by threonine induces autophosphorylating activity in GTP-binding domain of elongation factor Tu.

Pub. Date : 1990 Apr 25

PMID : 2157708






1 Functional Relationships(s)
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1 Mutation of Pro82 into Thr, a residue situated in the second element (D80CPG83) of the consensus sequence proposed to interact with GTP/GDP in GTP-binding proteins was introduced via site-directed mutagenesis in the isolated guanine nucleotide-binding domain (G domain) of elongation factor Tu. Guanine Nucleotides eukaryotic translation elongation factor 1 alpha 1 Homo sapiens