Structural mechanisms of QacR induction and multidrug recognition.

Article Details

Citation

Schumacher MA, Miller MC, Grkovic S, Brown MH, Skurray RA, Brennan RG

Structural mechanisms of QacR induction and multidrug recognition.

Science. 2001 Dec 7;294(5549):2158-63.

PubMed ID
11739955 [ View in PubMed
]
Abstract

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
HTH-type transcriptional regulator QacRP0A0N4Details