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Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489)

Acta Cryst. (2007). F63, 168–172 [doi:10.1107/S1744309107007221]

[Bacillus anthracis]The cyclo-ligase enzyme from Bacillus anthracis catalyzes the chemical conversion of 5-formyltetrahydrofolate (vitamin B9). A cut-through of the structure reveals an internal pocket, where the catalytic process occurs.
Bacillus anthracis, responsible for the life-threatening disease anthrax, has been used as an agent of bioterrorism. To provide information to underpin the discovery of new drugs against anthrax, we have analyzed the structure of a number of anthracis proteins as part of the Structural Proteomics in Europe initiative. We report the crystal structure of 5-formyltetrahydrofolate cyclo-ligase, an enzyme involved in regulating bacterial cell growth. The atomic-resolution structure gives a detailed picture of its catalytic mechanism and suggests how inhibitors of the enzyme might be designed.
C. Meier, L.G. Carter, G. Winter, R.J. Owens, D.I. Stuart and R.M. Esnouf