Publication | Closed Access
Structural Mechanisms of QacR Induction and Multidrug Recognition
367
Citations
26
References
2001
Year
Proteinlipid InteractionDrug TargetSignal RecognitionMolecular BiologyDrug ResistanceBioanalysisMolecular RecognitionAntimicrobial ResistanceProtein QacrBiochemistryMedicineStaphylococcus Aureus MultidrugPharmacologyStructural BiologyDna Bound StructureNatural SciencesQacr InductionRational Drug DesignElectrophysiologyChemical ProbeMolecular DockingDrug Discovery
The Staphylococcus aureus multidrug binding protein QacR represses transcription of the qacA multidrug transporter gene and is induced by structurally diverse cationic lipophilic drugs. Here, we report the crystal structures of six QacR-drug complexes. Compared to the DNA bound structure, drug binding elicits a coil-to-helix transition that causes induction and creates an expansive multidrug-binding pocket, containing four glutamates and multiple aromatic and polar residues. These structures indicate the presence of separate but linked drug-binding sites within a single protein. This multisite drug-binding mechanism is consonant with studies on multidrug resistance transporters.
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