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. doi: 10.1107/S2053230X14010164. Epub 2014 Jun 18.

Abstract

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.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Bacterial Secretion Systems / immunology
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Gene Expression
  • Molecular Weight
  • Pseudomonas aeruginosa / chemistry*
  • Pseudomonas aeruginosa / immunology
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Selenomethionine / chemistry*

Substances

  • Bacterial Proteins
  • Bacterial Secretion Systems
  • Recombinant Proteins
  • Selenomethionine