A preliminary X-ray study of a refolded PTS EIIBfruc protein from Escherichia coli.
The phosphoenolpyruvate-carbohydrate phosphotransferase system (PTS) catalyzes the phosphorylation and transportation of its sugar substrates. A sugar-specific enzyme II complex involved in the PTS finally functions to translocate substrates across the membrane. A PTS EIIB(fruc) protein, a fructose specific EIIB subunit, from Escherichia coli has been cloned, expressed, refolded, purified, and crystallized. The synchrotron data were collected to 2.6 A from the crystal of a selenomethionine substitute PTS EIIB(fruc) protein. The crystal belongs to the primitive trigonal space group P3(1)21, with unit-cell parameters of a = 33.4 A, b = 33.4 A, c = 154.0 A, and beta = 120.0 degrees . A full structure determination is under way to provide insights into the structure-function relationships of this protein.
Shin
Dong Hae
DH
College of Pharmacy, Ewha Womans University, Seoul 120-750, Korea. dhshin55@ewha.ac.kr
D018360:Crystallography, X-Ray / Q000379:methods; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D005632:Fructose / Q000378:metabolism*; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D017356:Synchrotrons
D029968:Escherichia coli Proteins; D021122:Protein Subunits; D005632:Fructose; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System