Back to Search
Start Over
Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489).
- Source :
-
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2007 Mar 01; Vol. 63 (Pt 3), pp. 168-72. Date of Electronic Publication: 2007 Feb 23. - Publication Year :
- 2007
-
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.
- Subjects :
- Adenosine Diphosphate chemistry
Amino Acid Sequence
Bacterial Proteins isolation & purification
Carbon-Nitrogen Ligases isolation & purification
Catalytic Domain
Crystallography, X-Ray methods
Magnesium chemistry
Protein Structure, Secondary
Protein Structure, Tertiary
Bacillus anthracis enzymology
Bacterial Proteins chemistry
Carbon-Nitrogen Ligases chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1744-3091
- Volume :
- 63
- Issue :
- Pt 3
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section F, Structural biology and crystallization communications
- Publication Type :
- Academic Journal
- Accession number :
- 17329806
- Full Text :
- https://doi.org/10.1107/S1744309107007221