Abstract
Bacillus anthracis is a spore-forming bacterium and the causative agent of the disease anthrax. The Oxford Protein Production Facility has been targeting proteins from B. anthracis in order to develop high-throughput technologies within the Structural Proteomics in Europe project. As part of this work, the structure of 5-formyltetrahydrofolate cyclo-ligase (BA4489) has been determined by X-ray crystallography to 1.6 Å resolution. The structure, solved in complex with magnesium-ion-bound ADP and phosphate, gives a detailed picture of the proposed catalytic mechanism of the enzyme. Chemical differences from other cyclo-ligase structures close to the active site that could be exploited to design specific inhibitors are also highlighted. © International Union of Crystallography 2007.
Author supplied keywords
Cite
CITATION STYLE
Meier, C., Carter, L. G., Winter, G., Owens, R. J., Stuart, D. I., & Esnouf, R. M. (2007). Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489). Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 63(3), 168–172. https://doi.org/10.1107/S1744309107007221
Register to see more suggestions
Mendeley helps you to discover research relevant for your work.