嗜肺军团菌 T2SS 效应蛋白 Lpg0189 的晶体结构揭示了一种新的蛋白质折叠方式。
Crystal structure of a hypothetical T2SS effector Lpg0189 from Legionella pneumophila reveals a novel protein fold.
机构信息
Institute of Physical Science and Information Technology, Anhui University, Hefei, Anhui, 230601, China; School of Chemistry and Chemical Engineering, Anhui University, Hefei, Anhui, 230601, China.
Institute of Physical Science and Information Technology, Anhui University, Hefei, Anhui, 230601, China.
出版信息
Biochem Biophys Res Commun. 2020 Jan 15;521(3):799-805. doi: 10.1016/j.bbrc.2019.10.195. Epub 2019 Nov 6.
Lpg0189 is a type II secretion system-dependent extracellular protein with unknown function from Legionella pneumophila. Herein, we determined the crystal structure of Lpg0189 at 1.98 Å resolution by using single-wavelength anomalous diffraction (SAD). Lpg0189 folds into a novel chair-shaped architecture, with two sheets roughly perpendicular to each other. Bioinformatics analysis suggests Lpg0189 and its homologues are unique to Legionellales and evolved divergently. The interlinking structural and bioinformatics studies provide a better understanding of this hypothetical protein.
Lpg0189 是来自嗜肺军团菌的 II 型分泌系统依赖的细胞外未知功能蛋白。在此，我们通过单波长反常散射（SAD）确定了 Lpg0189 的晶体结构，分辨率为 1.98 Å。Lpg0189 折叠成一种新颖的椅子形结构，两个大致相互垂直的片层。生物信息学分析表明，Lpg0189 及其同源物是军团菌目的特有蛋白，并且进化上存在分歧。结构和生物信息学的相互关联研究提供了对这种假设蛋白的更好理解。
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