Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 63, Part 3 (March 2007)

protein structure communications

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

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

C. Meier, L. G. Carter, G. Winter, R. J. Owens, D. I. Stuart and R. M. Esnouf

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.

PDB reference: 2jcb

Keywords: 5,10-methenyltetrahydrofolate synthetase; MTHFS.