Journal
SCIENCE
Volume 294, Issue 5549, Pages 2158-2163Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1066020
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- NIAID NIH HHS [AI 48593] Funding Source: Medline
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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 muttisite drug-binding mechanism is consonant with studies on multidrug resistance transporters.
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