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Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance

Item Type:Article
Title:Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance
Creators Name:Hinrichs, W. and Kisker, C. and Duevel, M. and Mueller, A. and Tovar, K. and Hillen, W. and Saenger, W.
Abstract:The most frequently occurring resistance of Gram-negative bacteria against tetracyclines is triggered by drug recognition of the Tet repressor. This causes dissociation of the repressor-operator DNA complex and enables expression of the resistance protein TetA, which is responsible for active efflux of tetracycline. The 2.5 angstrom resolution crystal structure of the homodimeric Tet repressor complexed with tetracycline-magnesium reveals detailed drug recognition. The orientation of the operator-binding helix-turn-helix motifs of the repressor is inverted in comparison with other DNA binding proteins. The repressor-drug complex is unable to interact with DNA because the separation of the DNA binding motifs is 5 angstroms wider than usually observed.
Keywords:Antiporters, Bacterial Proteins, X-Ray Crystallography, Bacterial DNA, Helix-Loop-Helix Motifs, Hydrogen Bonding, Magnesium, Molecular Models, Mutation, Genetic Operator Regions, Genetic, Protein Folding, Secondary Protein Structure, Repressor Proteins, Tetracycline, Tetracycline Resistance
Publisher:American Association for the Advancement of Science
Page Range:418-420
Date:15 April 1994
Official Publication:https://doi.org/10.1126/science.8153629
PubMed:View item in PubMed

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