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 language||English (US)|
|Number of pages||5|
|Journal||Antimicrobial agents and chemotherapy|
|State||Published - 1993|
ASJC Scopus subject areas
- Pharmacology (medical)
- Infectious Diseases