A Preliminary X-Ray Study of a Refolded PTS EIIBfruc Protein from Escherichia coli

Title: A Preliminary X-Ray Study of a Refolded PTS EIIBfruc Protein from Escherichia coli

Volume: 15 Issue: 6

Author(s): Dong Hae Shin

Affiliation:

Keywords: Phosphoenolpyruvate-carbohydrate phosphotransferase system, a fructose specific EIIB subunit, refolding, crystal, X-ray

Abstract: 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 EIIBfruc 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 Å from the crystal of a selenomethionine substitute PTS EIIBfruc protein. The crystal belongs to the primitive trigonal space group P3121, with unit-cell parameters of a = 33.4 Å, b = 33.4 Å, c = 154.0 Å, and β = 120.0°. A full structure determination is under way to provide insights into the structure-function relationships of this protein.

Cite this article as:

Shin Hae Dong, A Preliminary X-Ray Study of a Refolded PTS EIIBfruc Protein from Escherichia coli, Protein & Peptide Letters 2008; 15 (6) . https://dx.doi.org/10.2174/092986608784967001