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


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 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.

SUBMITTER: Meier C 

PROVIDER: S-EPMC2330188 | biostudies-literature | 2007 Mar

REPOSITORIES: biostudies-literature

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

Meier Christoph C   Carter Lester G LG   Winter Graeme G   Owens Ray J RJ   Stuart David I DI   Esnouf Robert M RM  

Acta crystallographica. Section F, Structural biology and crystallization communications 20070223 Pt 3


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  ...[more]

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