The NH2-terminal Half of the Tn10-specified Tetracycline Efflux Protein TetA Contains a Dimerization Domain
نویسندگان
چکیده
منابع مشابه
Substitutions in the interdomain loop of the Tn10 TetA efflux transporter alter tetracycline resistance and substrate specificity.
Cysteine replacement of Asp190, Glu192 and Ser201 residues in the cytoplasmic interdomain loop of the TetA(B) tetracycline efflux antiporter from Tn10 reduces tetracycline resistance [Tamura, N., Konishi, S., Iwaki, S., Kimura-Someya, T., Nada, S. & Yamaguchi, A. (2001). J Biol Chem 276, 20330-20339]. It was found that these Cys substitutions altered the substrate specificity of TetA(B), increa...
متن کاملInterdomain loop mutation Asp190Cys of the tetracycline efflux transporter TetA(B) decreases affinity for substrate.
TetA(B), the tetracycline efflux protein from Tn10, has 12 predicted α-helices that span the Escherichia coli cytoplasmic membrane (10) and is a member of the Major Facilitator Superfamily (4). TetA(B) and related tetracycline antiporters use the bacterial transmembrane proton motive force to export one metal-tetracycline complex in exchange for one H + (12), thereby reducing the intracellular ...
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Tetracycline uptake into inverted membrane vesicles from Tn10-bearing Escherichia coli cells required divalent cations. The degree of the stimulation of tetracycline uptake by various divalent cations showed the following decreasing order: Co2+ greater than Mn2+ greater than Mg2+ greater than Cd2+ greater than Ca2+. This order is consistent with the increasing order of the dissociation constant...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1995
ISSN: 0021-9258
DOI: 10.1074/jbc.270.39.22752