期刊
BIOPHYSICAL CHEMISTRY
卷 115, 期 2-3, 页码 229-233出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bpc.2004.12.032
关键词
circular dichroism; enzyme I of the bacterial phosphoenol pyruvate : sugar phosphotransferase system; Fourier transform infrared spectroscopy; thermal unfolding
The bacterial phosphoenolpyruvate (PEP): sugar phosphotransferase system (PTS), formed by a cascade of several proteins, couples the translocation and phosphorylation of specific sugars across cell membranes. The structure and thermal stability of the first protein (enzyme I, El) of the PTS in Streptomyces coelicolor is studied by using far-UV circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR) at pH 7.0. The deconvolution of FTIR spectra indicates that the protein is mainly composed by a 35% of a-helical structure and 30% of beta-sheet. The thermal denaturation curves, as followed by both techniques, show only a midpoint at 330 K. This thermal denaturation behaviour is different to that observed in other members of the El family. (c) 2004 Elsevier B.V. All rights reserved.
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