Latvian Biomedical Research and Study Centre, Riga, Latvia.
Latvian Institute of Organic Synthesis, Riga, Latvia.
FEBS Lett. 2020 Jan;594(2):317-326. doi: 10.1002/1873-3468.13594. Epub 2019 Sep 13.
The periplasmic lipoprotein BB0365 of the Lyme disease agent Borrelia burgdorferi is expressed throughout mammalian infection and is essential for all phases of Lyme disease infection; its function, however, remains unknown. In the current study, our structural analysis of BB0365 revealed the same structural fold as that found in the NqrC and RnfG subunits of the NADH:quinone and ferredoxin:NAD sodium-translocating oxidoreductase complexes, which points to a potential role for BB0365 as a component of the sodium pump. Additionally, BB0365 coordinated Zn by the His51, His55, His140 residues, and the Zn -binding site indicates that BB0365 could act as a potential metalloenzyme; therefore, this structure narrows down the potential functions of BB0365, an essential protein for B. burgdorferi to cause Lyme disease.
伯氏疏螺旋体（Borrelia burgdorferi）中莱姆病病原体的周质脂蛋白 BB0365 在整个哺乳动物感染过程中表达，是莱姆病感染所有阶段所必需的；但其功能仍然未知。在当前的研究中，我们对 BB0365 的结构分析揭示了与 NADH：醌和铁氧还蛋白：NAD 钠转运氧化还原酶复合物的 NqrC 和 RnfG 亚基中发现的相同结构折叠，这表明 BB0365 可能作为钠泵的一个组成部分发挥作用。此外，BB0365 通过 His51、His55 和 His140 残基协调 Zn，并显示 Zn 结合位点表明 BB0365 可以作为一种潜在的金属酶发挥作用；因此，该结构缩小了 BB0365 的潜在功能，BB0365 是伯氏疏螺旋体引起莱姆病的必需蛋白。
