Bacterial Metal Resistance: Coping with Copper without Cooperativity?

Bacterial Metal Resistance: Coping with Copper without Cooperativity?
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DOI:
10.1128/mbio.00653-21
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发表时间:
2021-06-29
期刊:
影响因子:
6.4
通讯作者:
Koronakis V
Koronakis V
中科院分区:
生物学1区
文献类型:
--
作者:
Greene NP;Koronakis V

文献摘要

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在大肠杆菌和其他革兰氏阴性细菌中,三部分外排泵(TEPs)跨越整个细胞包膜,用于从细胞中清除有害分子。CusBCA是一种TEP,在大肠杆菌中负责铜和银的解毒。大肠杆菌的抗性-增殖-细胞分裂(RND)转运蛋白CusA。在最近的一项研究中,Moseng等人(M. A.莫森湾柳氏T. Pipatpolkai,P. Glaza等人,mBio 12:e00452-21,2021,https://dx. doi. org/10. 1128/mBio.00452 - 21)在铜存在下获得了CustA三聚体的低温电子显微镜(cryo-EM)结构。揭示的多种构象表明,这三个单体的功能独立内的CusA三聚体,相反的合作机制提出的多药出口RND转运蛋白,AcrB。这项工作促使人们考虑这类转运蛋白的机制,并为进一步研究对细菌生存至关重要的TEPs提供了基础。
In Escherichia coli and other Gram-negative bacteria, tripartite efflux pumps (TEPs) span the entire cell envelope and serve to remove noxious molecules from the cell. CusBCA is a TEP responsible for copper and silver detoxification in E. coli powered by the resistance-nodulation-cell division (RND) transporter, CusA. In a recent study, Moseng et al. (M. A. Moseng, M. Lyu, T. Pipatpolkai, P. Glaza, et al., mBio 12:e00452-21, 2021, https://dx.doi.org/10.1128/mBio.00452-21) obtained cryo-electron microscopy (cryo-EM) structures of CusA trimers in the presence of copper. The multiple conformations revealed suggest that the three monomers function independently within the CusA trimer, contrary to the cooperative mechanism proposed for the multidrug exporting RND transporter, AcrB. The work prompts consideration of the mechanism of this class of transporter and provides a basis to underpin further studies of TEPs important for bacterial survival.