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Journal of Bacteriology, December 2007, p. 9131-9134, Vol. 189, No. 24
0021-9193/07/$08.00+0     doi:10.1128/JB.01492-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Transmembrane Helix 12 of the Staphylococcus aureus Multidrug Transporter QacA Lines the Bivalent Cationic Drug Binding Pocket{triangledown}

Karl A. Hassan,1 Ronald A. Skurray,1 and Melissa H. Brown1,2*

School of Biological Sciences, The University of Sydney, Sydney, New South Wales, Australia,1 School of Biological Sciences, Flinders University, Adelaide, South Australia, Australia2

Received 17 September 2007/ Accepted 5 October 2007

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 that TMS 12 is a component of the bivalent cation-binding region.

* Corresponding author. Mailing address: School of Biological Sciences, Flinders University, Adelaide, South Australia, Australia 5001. Phone: 61 8 8201 2747. Fax: 61 8 8201 3015. E-mail: Melissa.Brown{at}flinders.edu.au

{triangledown} Published ahead of print on 19 October 2007.

Journal of Bacteriology, December 2007, p. 9131-9134, Vol. 189, No. 24
0021-9193/07/$08.00+0     doi:10.1128/JB.01492-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • 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]  


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