Suppr超能文献

细菌金属抗性:无协同作用应对铜?

Bacterial Metal Resistance: Coping with Copper without Cooperativity?

机构信息

Department of Pathology, University of Cambridge, Cambridge, United Kingdom.

出版信息

mBio. 2021 Jun 29;12(3):e0065321. doi: 10.1128/mBio.00653-21. Epub 2021 Jun 15.

Abstract

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.

摘要

在大肠杆菌和其他革兰氏阴性菌中,三部分流出泵(TEP)跨越整个细胞包膜,用于从细胞中去除有害物质。CusBCA 是一种 TEP,负责大肠杆菌中的铜和银解毒,由抗性-结节-细胞分裂(RND)转运蛋白 CusA 驱动。在最近的一项研究中,Moseng 等人(M. A. Moseng、M. Lyu、T. Pipatpolkai、P. Glaza 等,mBio 12:e00452-21, 2021, https://dx.doi.org/10.1128/mBio.00452-21)获得了铜存在下 CusA 三聚体的冷冻电镜(cryo-EM)结构。揭示的多种构象表明,三个单体在 CusA 三聚体中独立发挥作用,与多药物外排 RND 转运蛋白 AcrB 提出的合作机制相反。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很重要的 TEP 提供了基础。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验