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

Karl A. Hassan; Ronald A. Skurray; Melissa H. Brown

doi:10.1128/JB.01492-07

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

Karl A. Hassan, Ronald A. Skurray, Melissa H. Brown^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

15 Citations (Scopus)

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

Original language	English
Pages (from-to)	9131-9135
Number of pages	5
Journal	Journal of Bacteriology
Volume	189
Issue number	24
DOIs	https://doi.org/10.1128/JB.01492-07
Publication status	Published - Dec 2007
Externally published	Yes

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

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

author = "Hassan, {Karl A.} and Skurray, {Ronald A.} and Brown, {Melissa H.}",

year = "2007",

month = dec,

doi = "10.1128/JB.01492-07",

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volume = "189",

pages = "9131--9135",

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publisher = "American Society for Microbiology",

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AU - Hassan, Karl A.

AU - Skurray, Ronald A.

AU - Brown, Melissa H.

PY - 2007/12

Y1 - 2007/12

N2 - 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.

AB - 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.

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U2 - 10.1128/JB.01492-07

DO - 10.1128/JB.01492-07

M3 - Article

C2 - 17951386

AN - SCOPUS:37449027379

SN - 0021-9193

VL - 189

SP - 9131

EP - 9135

JO - Journal of Bacteriology

JF - Journal of Bacteriology

IS - 24

ER -

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

Abstract

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