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双 BON 结构域蛋白 DolP 的结构鉴定出磷脂结合是一种新的蛋白质定位机制。

Structure of dual BON-domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation.

机构信息

Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom.

School of Biosciences, University of Birmingham, Edgbaston, United Kingdom.

出版信息

Elife. 2020 Dec 14;9:e62614. doi: 10.7554/eLife.62614.

DOI:10.7554/eLife.62614
PMID:33315009
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7806268/
Abstract

The Gram-negative outer-membrane envelops the bacterium and functions as a permeability barrier against antibiotics, detergents, and environmental stresses. Some virulence factors serve to maintain the integrity of the outer membrane, including DolP (formerly YraP) a protein of unresolved structure and function. Here, we reveal DolP is a lipoprotein functionally conserved amongst Gram-negative bacteria and that loss of DolP increases membrane fluidity. We present the NMR solution structure for DolP, which is composed of two BON domains that form an interconnected opposing pair. The C-terminal BON domain binds anionic phospholipids through an extensive membrane:protein interface. This interaction is essential for DolP function and is required for sub-cellular localisation of the protein to the cell division site, providing evidence of subcellular localisation of these phospholipids within the outer membrane. The structure of DolP provides a new target for developing therapies that disrupt the integrity of the bacterial cell envelope.

摘要

革兰氏阴性外膜包裹着细菌，作为抗生素、去污剂和环境压力的渗透性屏障。一些毒力因子有助于维持外膜的完整性，包括 DolP（以前称为 YraP），一种结构和功能尚未确定的蛋白质。在这里，我们揭示了 DolP 是革兰氏阴性细菌中具有保守功能的脂蛋白，并且 DolP 的缺失会增加膜的流动性。我们提出了 DolP 的 NMR 溶液结构，它由两个 BON 结构域组成，形成相互连接的对立对。C 端 BON 结构域通过广泛的膜：蛋白界面与阴离子磷脂结合。这种相互作用对于 DolP 的功能至关重要，并且是蛋白质亚细胞定位到细胞分裂部位所必需的，这为这些磷脂在质膜内的亚细胞定位提供了证据。DolP 的结构为开发破坏细菌细胞外膜完整性的治疗方法提供了一个新的靶点。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fc24/7806268/a8a958cc952b/elife-62614-fig3-figsupp3.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fc24/7806268/f0ec8b82c67b/elife-62614-fig1.jpg
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