Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489)
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
![[Bacillus anthracis]](https://www.iucr.org/__data/assets/image/0005/4649/ActaF.gif)
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.
