Defining the epitope region of a peptide from the Streptomyces coelicolor phosphoenolpyruvate:sugar phosphotransferase system able to bind to the enzyme I.

ABSTRACT: The bacterial PEP:sugar PTS consists of a cascade of several proteins involved in the uptake and phosphorylation of carbohydrates, and in signal transduction pathways. Its uniqueness in bacteria makes the PTS a target for new antibacterial drugs. These drugs can be obtained from peptides or protein fragments able to interfere with the first reaction of the protein cascade: the phosphorylation of the HPr by the first enzyme, the so-called enzyme EI. To that end, we designed a peptide, HPr(9-30), spanning residues 9 to 30 of the intact HPr protein, containing the active site histidine (His-15) and the first alpha-helix of HPr of Streptomyces coelicolor, HPr(sc). By using fluorescence and circular dichroism, we first determined qualitatively that HPr(sc) and HPr(9-30) did bind to EI(sc), the

SUBMITTER: Hurtado-Gomez E 

PROVIDER: S-EPMC2479611 | biostudies-literature | 2008 Aug

REPOSITORIES: biostudies-literature