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J. Bacteriol. doi:10.1128/JB.01492-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Transmembrane helix 12 of the Staphylococcus aureus multidrug transporter QacA lines the bivalent cationic drug binding pocket

School of Biological Sciences, The University of Sydney, Sydney, New South Wales, Australia, School of Biological Sciences, Flinders University, Adelaide, South Australia, Australia

^* To whom correspondence should be addressed. Email: Melissa.Brown{at}flinders.edu.au.

	Abstract

An acidic residue in transmembrane segment (TMS) 10 is important for recognition of bivalent cationic substrates by the QacA multidrug transporter. Remarkably, an acidic residue in TMS 12 compensated for the absence of such a residue in TMS 10, suggesting TMS 12 is a component of the bivalent cation binding region.

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• Hassan, K. A., Souhani, T., Skurray, R. A., Brown, M. H. (2008). Analysis of Tryptophan Residues in the Staphylococcal Multidrug Transporter QacA Reveals Long-Distance Functional Associations of Residues on Opposite Sides of the Membrane. J. Bacteriol. 190: 2441-2449 [Abstract] [Full Text]