有哪些信誉好的足球投注网站a single acidic residue can guide binding site selection but does not govern qacr cationic-drug affinity一个酸性渣可以指导结合位点选择但不治理qacr cationic-drug亲和力.pdfVIP
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a single acidic residue can guide binding site selection but does not govern qacr cationic-drug affinity一个酸性渣可以指导结合位点选择但不治理qacr cationic-drug亲和力
A Single Acidic Residue Can Guide Binding Site Selection
but Does Not Govern QacR Cationic-Drug Affinity
1. 2. 2¤ 1
Kate M. Peters , Benjamin E. Brooks , Maria A. Schumacher , Ronald A. Skurray , Richard G.
Brennan2*¤, Melissa H. Brown1,3*
1 School of Biological Sciences, University of Sydney, Sydney, New South Wales, Australia, 2 Department of Biochemistry and Molecular Biology, MD Anderson Cancer
Centre Houston, Texas, United States of America, 3 School of Biological Sciences, Flinders University, Adelaide, South Australia, Australia
Abstract
Structures of the multidrug-binding repressor protein QacR with monovalent and bivalent cationic drugs revealed that the
carboxylate side-chains of E90 and E120 were proximal to the positively charged nitrogens of the ligands ethidium,
malachite green and rhodamine 6G, and therefore may contribute to drug neutralization and binding affinity. Here, we
report structural, biochemical and in vivo effects of substituting these glutamate residues. Unexpectedly, substitutions had
little impact on ligand affinity or in vivo induction capabilities. Structures of QacR(E90Q) and QacR(E120Q) with ethidium or
malachite green took similar global conformations that differed significantly from all previously described QacR-drug
complexes but still prohibited binding to cognate DNA. Strikingly, the QacR(E90Q)-rhodamine 6G complex revealed two
mutually exclusive rhodamine 6G binding sites. Despite multiple structural changes, all drug binding was essentially
isoenergetic. Thus, these data strongly suggest that rather tha
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