Site-Directed Mutagenesis Studies of Selected Motif and Charged Residues and of Cysteines of the Multifunctional Tetracycline Efflux Protein Tet(L)
Open Access
- 15 March 2002
- journal article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 184 (6) , 1796-1800
- https://doi.org/10.1128/jb.184.6.1796-1800.2002
Abstract
All of the transmembrane glutamates of Tet(L) are essential for tetracycline (TET) resistance, and E397 has been shown to be essential for all catalytic modes, i.e., TET-Me 2+ and Na + efflux and K + uptake. Loop residues D74 and G70 are essential for TET flux but not for Na + or K + flux. A cysteineless Tet(L) protein exhibits all activities.Keywords
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