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 language | English (US) |
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Pages (from-to) | 2645-2649 |
Number of pages | 5 |
Journal | Antimicrobial agents and chemotherapy |
Volume | 37 |
Issue number | 12 |
DOIs | |
State | Published - 1993 |
ASJC Scopus subject areas
- Pharmacology
- Pharmacology (medical)
- Infectious Diseases