Structure and mechanism of the bacterial lipid ABC transporter, MlaFEDB.

Structure and mechanism of the bacterial lipid ABC transporter, MlaFEDB.
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DOI:
10.1016/j.sbi.2022.102429
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发表时间:
2022-10
影响因子:
6.8
通讯作者:
Bhabha G
Bhabha G
中科院分区:
生物学2区
文献类型:
--
作者:
Ekiert DC;Coudray N;Bhabha G

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革兰氏阴性细菌的细胞膜由内膜、外膜和中间的周质空间组成。外膜脂质如何在那里运输和组装,以及如何维持外膜的不对称性是一个深入研究的领域。 Mla 系统与外膜脂质不对称性的维持有关,并且通常被认为驱动从外膜去除错误定位的磷脂并将其逆行转运至内膜。 Mla 通路的核心是内膜中结构独特的 ABC 转运蛋白复合物,称为 MlaFEDB。最近,大量冷冻电镜研究开始揭示 MlaFEDB 的结构和脂质易位机制,它与其他 ABC 转运蛋白家族(包括人类 ABCA 和 ABCG,以及细菌脂多糖和 O 抗原转运蛋白)有许多相似之处。在这里,我们综合了所有可用结构的信息,并提出了 MlaFEDB 跨细胞包膜脂质运输的模型。
The cell envelope of Gram-negative bacteria is composed of an inner membrane, outer membrane and an intervening periplasmic space. How the outer membrane lipids are trafficked and assembled there, and how the asymmetry of the outer membrane is maintained is an area of intense research. The Mla system has been implicated in the Maintenance of Lipid Asymmetry in the outer membrane, and is generally thought to drive the removal of mislocalized phospholipids from the outer membrane and their retrograde transport to the inner membrane. At the heart of the Mla pathway is an structurally unique ABC transporter complex in the inner membrane, called MlaFEDB. Recently, an explosion of cryo-EM studies has begun to shed light on the structure and lipid translocation mechanism of MlaFEDB, with many parallels to other ABC transporter families, including human ABCA and ABCG, as well as bacterial lipopolysaccharide and O-antigen transporters. Here we synthesize information from all available structures, and propose a model for lipid trafficking across the cell envelope by MlaFEDB.
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