title: Site-directed mutagenesis studies of selected motif and charged residues and of cysteines of the multifunctional tetracycline efflux protein Tet(L).
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.
authors.affiliation: Department of Pharmacology and Biological Chemistry, Mount Sinai School of Medicine, New York, New York 10029, USA.
authors.forename: Jie
authors.initials: J
authors.lastname: Jin
authors.forename: Terry A
authors.initials: TA
authors.lastname: Krulwich
mesh_terms: D017920:Antiporters / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D003545:Cysteine / Q000235:genetics*; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins; D005971:Glutamates / Q000378:metabolism; D017136:Ion Transport; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D016297:Mutagenesis, Site-Directed; D011188:Potassium / Q000378:metabolism; D012964:Sodium / Q000378:metabolism; D013753:Tetracycline Resistance / Q000235:genetics
chemical_list: D017920:Antiporters; D029968:Escherichia coli Proteins; D005971:Glutamates; D008565:Membrane Proteins; C424711:Tet(L) protein, E coli; D012964:Sodium; D003545:Cysteine; D011188:Potassium