Waste or die: The price to pay to stay alive

被引:8
|
作者
Orelle, Cedric [1 ]
Schmitt, Lutz [2 ]
Jault, Jean-Michel [1 ]
机构
[1] Univ Lyon, CNRS, Mol Microbiol & Struct Biochem, IBCP,UMR5086, 7 Passage Vercors, F-69367 Lyon, France
[2] Heinrich Heine Univ, Inst Biochem, Univ Str 1, D-40225 Dusseldorf, Germany
关键词
HETERODIMERIC ABC TRANSPORTER; P-GLYCOPROTEIN; MULTIDRUG TRANSPORTER; ATP-BINDING; CONFORMATIONAL-CHANGES; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; STRUCTURAL BASIS; DRUG-BINDING; MECHANISM;
D O I
10.1016/j.tim.2022.09.005
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Microorganisms need to constantly exchange with their habitat to capture nutri-ents and expel toxic compounds. The ATP-binding cassette (ABC) transporters, a family of membrane proteins especially abundant in microorganisms, are at the core of these processes. Due to their extraordinary ability to expel structurally unrelated compounds, some transporters play a protective role in different or-ganisms. Yet, the downside of these multidrug transporters is their entanglement in the resistance to therapeutic treatments. Intriguingly, some multidrug ABC transporters show a high level of ATPase activity, even in the absence of transported substrates. Although this basal ATPase activity might seem a waste, we surmise that this inherent capacity allows multidrug transporters to promptly translocate any bound drug before it penetrates into the cell.
引用
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页码:233 / 241
页数:9
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