Structural analysis of Borrelia burgdorferi periplasmic lipoprotein BB0365 involved in Lyme disease infection
Structural analysis of Borrelia burgdorferi periplasmic lipoprotein BB0365 involved in Lyme disease infection
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DOI：
10.1002/1873-3468.13594
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发表时间：
2019-09-13
期刊：
影响因子：
3.5
通讯作者：
Tars, Kaspars
中科院分区：
文献类型：
--
作者：
Brangulis, Kalvis;Akopjana, Inara;Tars, Kaspars
莱姆病病原体伯氏疏螺旋体的周质脂蛋白BB 0365在整个哺乳动物感染中表达，并且对于莱姆病感染的所有阶段都是必需的;然而，其功能仍然未知。在当前的研究中，我们对BB 0365的结构分析揭示了与在NADH：醌和铁氧还蛋白：NAD（+）钠转运氧化还原酶复合物的NqrC和RnfG亚基中发现的相同的结构折叠，这指出了BB 0365作为钠泵组分的潜在作用。此外，BB 0365通过His 51、His 55、His 140残基和Zn 2+结合位点与Zn 2+配位，表明BB 0365可以作为潜在的金属酶;因此，这种结构缩小了BB 0365（B的必需蛋白）的潜在功能。莱姆病的病原体。
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 Zn2+ by the His51, His55, His140 residues, and the Zn2+-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.