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Article

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

The Journal of biological chemistry - 25 Apr 1990

Cool R H, Jensen M, Jonák J, Clark B F, Parmeggiani A

Abstract excerpt

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. G domainPT82 displays virtually no GTPase activity. As a major change, the apparent inhibition of the GTPase reaction is...

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PMID: 2157708

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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