The structure of DcrB, a lipoprotein from Salmonella enterica, reveals flexibility in the N-terminal segment of the Mog1p/PsbP-like fold.

The structure of DcrB, a lipoprotein from Salmonella enterica, reveals flexibility in the N-terminal segment of the Mog1p/PsbP-like fold.
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DOI:
10.1016/j.jsb.2018.10.005
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发表时间:
2018-12
影响因子:
3
通讯作者:
May, John F.
May, John F.
中科院分区:
生物学3区
文献类型:
--
作者:
Rasmussen, Damien M.;Soens, Ross W.;Davie, Timothy J.;Vaneerd, Cody K.;Bhattacharyya, Basudeb;May, John F.

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DcrB是一种18千道尔顿的脂蛋白,含有一个功能未知的结构域。DcrB在肠杆菌科中发现,肠杆菌科是革兰氏阴性菌家族,包括可引起食源性疾病和医院获得性感染的病原体。在鼠伤寒沙门氏菌中,DcrB在促进已知毒力因子产生的条件下上调。我们确定了结构的截断形式的DcrB沙门氏菌的1.92纳米分辨率的X-射线晶体学。这种截短形式DcrBΔ37包含未知功能的整个结构域,但缺乏脂蛋白信号序列(残基1-20)以及残基21-37。DcrBΔ37单体含有Mog 1 p/PsbP样折叠,其在哺乳动物、酵母、植物和蓝藻中的功能多样的蛋白质中发现。有趣的是,DcrBΔ37结晶为结构域交换的同源二聚体,其中N-末端β-发夹从一个原聚体延伸,与第二个原聚体的核心相互作用。这种结构域交换表明Mog 1 p/PsbP样折叠的N-末端部分可能具有构象灵活性。总的来说,我们的研究结果提供了第一个例子的肠细菌蛋白,包含Mog 1 p/PsbP样折叠和扩展知识的Mog 1 p/PsbP样蛋白的结构和系统发育多样性。
DcrB is an 18 kilodalton lipoprotein that contains a single domain of unknown function. DcrB is found within Enterobacteriaceae, a family of Gram-negative bacteria which includes pathogens that can cause food-borne illness and hospital-acquired infections. In Salmonella enterica serovar Typhimurium, DcrB is up-regulated by conditions that promote the production of known virulence factors. We determined the structure of a truncated form of DcrB from Salmonella to 1.92 Å resolution by X-ray crystallography. This truncated form, DcrBΔ37, contains the entire domain of unknown function but lacks the lipoprotein signal sequence (residues 1–20) as well as residues 21–37. The DcrBΔ37 monomer contains the Mog1p/PsbP-like fold, which is found in functionally diverse proteins in mammals, yeast, plants, and cyanobacteria. Interestingly, DcrBΔ37 crystallized as a domain-swapped homodimer in which the N-terminal β-hairpin extends from one protomer to interact with the core of the second protomer. This domain-swapping indicates that the N-terminal portion of the Mog1p/PsbP-like fold likely has conformational flexibility. Overall, our results provide the first example of an enterobacterial protein that contains the Mog1p/PsbP-like fold and expands knowledge of the structural and phylogenetic diversity of Mog1p/PsbP-like proteins.
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