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The crystal structure of 5-formyl-tetrahydrofolate cycloligase from Bacillus anthracis (BA4489)The crystal structure of 5-formyl-tetrahydrofolate cycloligase from Bacillus anthracis (BA4489)
Structural highlights
FunctionEvolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBacillus 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. Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489).,Meier C, Carter LG, Winter G, Owens RJ, Stuart DI, Esnouf RM Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Mar 1;63(Pt, 3):168-72. Epub 2007 Feb 23. PMID:17329806[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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