Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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
- ↑ Meier C, Carter LG, Winter G, Owens RJ, Stuart DI, Esnouf RM. Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489). Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Mar 1;63(Pt, 3):168-72. Epub 2007 Feb 23. PMID:17329806 doi:http://dx.doi.org/10.1107/S1744309107007221
