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 among 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 to anionic phospholipids through an extensive membrane:protein interface providing evidence of subcellular localization of these phospholipids within the outer membrane. This interaction is essential for DolP function and is required for sub-cellular localization of the protein to the cell division site. The structure of DolP provides a new target for developing therapies that disrupt the integrity of the bacterial cell envelope.

中文翻译：

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双BON域蛋白DolP的结构功能分析确定磷脂结合是蛋白定位的新机制

革兰氏阴性外膜将细菌包裹起来，并充当针对抗生素，清洁剂和环境压力的渗透屏障。一些毒力因子可用来维持外膜的完整性，包括DolP（以前称为YraP），一种结构和功能尚未解析的蛋白质。在这里，我们揭示DolP是一种在革兰氏阴性细菌中功能上保守的脂蛋白，DolP的缺失会增加膜的流动性。我们提出了DolP的NMR溶液结构，该结构由两个BON域组成，形成相互连接的相对对。C端BON结构域通过广泛的膜：蛋白界面与阴离子磷脂结合，提供了这些磷脂在外膜内的亚细胞定位的证据。这种相互作用对于DolP功能是必不可少的，并且对于蛋白质在细胞的亚细胞定位到细胞分裂位点是必需的。DolP的结构为开发破坏细菌细胞包膜完整性的疗法提供了新的靶标。