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Cloning, purification, crystallization and preliminary X-ray studies of the putative type VI secretion immunity protein Tli5 (PA5088) from Pseudomonas aeruginosa.

Acta Crystallogr F Struct Biol Commun. 2014 Jul;70(Pt 7):903-5. Epub 2014 Jun 18
Zhen Chen 1 , Zengqiang Gao 2 , Haidai Hu 3 , Jianhua Xu 2 , Heng Zhang 2 , Yuhui Dong 2
Zhen Chen 1 , Zengqiang Gao 2 , Haidai Hu 3 , Jianhua Xu 2 , Heng Zhang 2 , Yuhui Dong 2
+ et al

[No authors listed]

Author information
  • 1 School of Life Sciences, Anhui University, Hefei 230601, People's Republic of China.
  • 2 Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, People's Republic of China.
  • 3 Key Laboratory of Molecular Virology and Immunology, Institute Pasteur of Shanghai, Chinese Academy of Sciences, Shanghai 200025, People's Republic of China.

摘要

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.

KEYWORDS: PA5088, Pseudomonas aeruginosa

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