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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 A 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.

Original publication

DOI

10.1107/s1744309107007221

Type

Journal article

Journal

Acta crystallographica. Section F, Structural biology and crystallization communications

Publication Date

03/2007

Volume

63

Pages

168 - 172

Addresses

Oxford Protein Production Facility, The Henry Wellcome Building for Genomic Medicine, Oxford University, Roosevelt Drive, Oxford OX3 7BN, England.

Keywords

Bacillus anthracis, Magnesium, Carbon-Nitrogen Ligases, Bacterial Proteins, Adenosine Diphosphate, Crystallography, X-Ray, Amino Acid Sequence, Catalytic Domain, Protein Structure, Secondary, Protein Structure, Tertiary