1jus
|
Crystal structure of the multidrug binding transcriptional repressor QacR bound to rhodamine 6G
OverviewOverview
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.
About this StructureAbout this Structure
1JUS is a Single protein structure of sequence from Staphylococcus aureus with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structural mechanisms of QacR induction and multidrug recognition., Schumacher MA, Miller MC, Grkovic S, Brown MH, Skurray RA, Brennan RG, Science. 2001 Dec 7;294(5549):2158-63. PMID:11739955
Page seeded by OCA on Thu Feb 21 13:27:02 2008