Expression, purification, crystallization and preliminary crystallographic analysis of PA3885 (TpbA) from Pseudomonas aeruginosa PAO1.
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.
Tianjin Key Laboratory of Protein Science, College of Life Sciences, Nankai University, Tianjin 300071, People's Republic of China.
Wen
W
Yang
Kan
K
Li
Yuwei
Y
Bai
Ruimin
R
Zhou
Weihong
W
Zhou
Mark
M
Bartlam
D003460:Crystallization; D018360:Crystallography, X-Ray; D015870:Gene Expression; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D011550:Pseudomonas aeruginosa / Q000201:enzymology*
D017027:Protein Tyrosine Phosphatases