Crystal structure of enzyme I of the phosphoenolpyruvate sugar phosphotransferase system in the dephosphorylated state.

ABSTRACT: The bacterial phosphoenolpyruvate (PEP) sugar phosphotransferase system mediates sugar uptake and controls the carbon metabolism in response to carbohydrate availability. Enzyme I (EI), the first component of the phosphotransferase system, consists of an N-terminal protein binding domain (EIN) and a C-terminal PEP binding domain (EIC). EI transfers phosphate from PEP by double displacement via a histidine residue on EIN to the general phosphoryl carrier protein HPr. Here we report the 2.4 A crystal structure of the homodimeric EI from Staphylococcus aureus. EIN consists of the helical hairpin HPr binding subdomain and the phosphorylatable betaalpha phospho-histidine (P-His) domain. EIC folds into an (betaalpha)(8) barrel. The dimer interface of EIC buries 1833 A(2) of accessible surface pe

SUBMITTER: Oberholzer AE 

PROVIDER: S-EPMC2785159 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature