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Membrane Potential Is Required for MurJ Function
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DOI：10.1021/jacs.8b00942.png)
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摘要
En 中文
MurJ, the flippase that exports the bacterial cell wall monomer Lipid II to the periplasm, is a target for new antibiotics, which are desperately needed to treat Gram-negative infections. Quantitative methods to monitor MurJ activity are required to characterize inhibitors but are challenging to develop because the lipid-linked substrate is not chemically altered in a flippase reaction. Here we show that MurJ inhibition can be quantified by measuring the accumulation of intracellular Lipid II using a biotin-tagging strategy. We have exploited this assay to show that MurJ is inhibited in the presence of a compound that dissipates the membrane potential. By probing cysteine accessibility we have found that under this condition MurJ relaxes into an inactive, outward-facing conformation reminiscent of that targeted by the peptide antibiotic Lys(M). We condude that membrane potential is required for MurJ function in E. coli, and we anticipate that the ability to accumulate this inactive conformation will lead to structures useful for inhibitor design.
Keyword:
LIPID II FLIPPASE
LINKED PEPTIDOGLYCAN
CRYSTAL-STRUCTURE
MULTIDRUG
EXTRUSION
MECHANISM
IDENTIFICATION
PRECURSORS
RESIDUES
ASSAY
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期刊
IF:
15.6
论文数:
20.0W
被引数:
60.2W
机构
引用论文
Bioinformatics identification of MurJ (MviN) as the peptidoglycan lipid II flippase in Escherichia coli大肠杆菌中MurJ (MviN) 作为肽聚糖脂质II翻转酶的生物信息学鉴定OAAI
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