Expression, purification, crystallization and preliminary crystallographic analysis of PA3885 (TpbA) from Pseudomonas aeruginosa PAO1.

Acta Crystallogr Sect F Struct Biol Cryst Commun

Tianjin Key Laboratory of Protein Science, College of Life Sciences, Nankai University, Tianjin 300071, People's Republic of China.

Published: November 2010

AI Article Synopsis

  • Biofilms play a key role in bacterial communication and growth, contributing to many human infections and diseases.
  • Quorum-sensing systems are essential for biofilm formation, with PA3885 (TpbA) in Pseudomonas aeruginosa converting these signals into reactions that lower biofilm production.
  • PA3885 was expressed, purified, and crystallized for X-ray crystallography; however, the precise protein arrangement in the crystals remains undetermined, and efforts to clarify its structure are ongoing.

Article Abstract

Biofilms are important in cell communication and growth in most bacteria and are also responsible for most human clinical infections and diseases. Quorum-sensing systems have been identified to be crucial for biofilm formation and regulation. PA3885 (TpbA), a tyrosine phosphatase, is reported to convert extracellular quorum-sensing signals into internal gene-cascade reactions that result in reduced biofilm formation in the opportunistic pathogen Pseudomonas aeruginosa. Here, PA3885 from P. aeruginosa PAO1 was expressed, purified and crystallized. Single crystals were studied by X-ray crystallography and native diffraction data were collected to 2.8 Å resolution. These crystals were determined to belong to space group C2. It was not possible to conclusively determine the number of proteins in the asymmetric unit from the preliminary X-ray diffraction data analysis alone and attempts to determine the crystal structure of PA3885 are currently under way.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3001651PMC
http://dx.doi.org/10.1107/S1744309110034317DOI Listing

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