铜绿假单胞菌假定的VI型分泌免疫蛋白Tli5（PA5088）的克隆、纯化、结晶及初步X射线研究
Cloning, purification, crystallization and preliminary X-ray studies of the putative type VI secretion immunity protein Tli5 (PA5088) from Pseudomonas aeruginosa.
作者信息
Chen Zhen, Gao Zengqiang, Hu Haidai, Xu Jianhua, Zhang Heng, Dong Yuhui
机构信息
School of Life Sciences, Anhui University, Hefei 230601, People's Republic of China.
Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, People's Republic of China.
出版信息
Acta Crystallogr F Struct Biol Commun. 2014 Jul;70(Pt 7):903-5. doi: 10.1107/S2053230X14010164. Epub 2014 Jun 18.
The putative protein PA5089 from Pseudomonas aeruginosa has recently been identified as a Tle5 phospholipase effector from a type VI secretion system (T6SS), and its toxicity can be neutralized by the cognate immunity protein Tli5 (PA5088). Here, the expression, purification, crystallization and preliminary crystallographic analysis of PA5088 are reported. X-ray diffraction data were collected from selenomethionine-derivatized PA5088 crystals to a resolution of 2.55 Å. The crystals belonged to space group P2₁, with unit-cell parameters a=64.002, b=104.744, c=90.168 Å.
最近，来自铜绿假单胞菌的假定蛋白PA5089被鉴定为VI型分泌系统（T6SS）的Tle5磷脂酶效应蛋白，其毒性可被同源免疫蛋白Tli5（PA5088）中和。本文报道了PA5088的表达、纯化、结晶及初步晶体学分析。从硒代甲硫氨酸衍生化的PA5088晶体收集X射线衍射数据，分辨率为2.55 Å。晶体属于空间群P2₁，晶胞参数a=64.002、b=104.744、c=90.168 Å。
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