Effect of mutational alteration of Asn-128 in the putative GTP-binding domain of tetracycline resistance determinant Tet(O) from Campylobacter jejuni

J. Grewal, E. K. Manavathu, D. E. Taylor

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

The deduced amino acid sequence of Campylobacter jejuni Tet(O), cloned in Escherichia coli, has shown that it contains the five highly conserved sequences of the GTP-binding domain found in other GTPases. Asn-128 belongs to the G4 motif of such a domain and is involved in hydrogen bonding with the guanine ring of the nucleotide. Substitution of Asn-128 by 11 other amino acids resulted in a decrease in tetracycline resistance, indicating that tetracycline resistance conferred by Tet(O) is related to GTP binding. The effect of the mutations on the GTP-binding domain is discussed with the EF- Tu-GDP complex as a model.

Original languageEnglish (US)
Pages (from-to)2645-2649
Number of pages5
JournalAntimicrobial agents and chemotherapy
Volume37
Issue number12
DOIs
StatePublished - 1993

ASJC Scopus subject areas

  • Pharmacology
  • Pharmacology (medical)
  • Infectious Diseases

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