Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489).
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.
Meier
Christoph
C
Oxford Protein Production Facility, The Henry Wellcome Building for Genomic Medicine, Oxford University, Roosevelt Drive, Oxford OX3 7BN, England.
Carter
Lester G
LG
Winter
Graeme
G
Owens
Ray J
RJ
Stuart
David I
DI
Esnouf
Robert M
RM
D000244:Adenosine Diphosphate / Q000737:chemistry; D000595:Amino Acid Sequence; D001408:Bacillus anthracis / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D019731:Carbon-Nitrogen Ligases / Q000737:chemistry* / Q000302:isolation & purification; D020134:Catalytic Domain; D018360:Crystallography, X-Ray / Q000379:methods; D008274:Magnesium / Q000737:chemistry; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D001426:Bacterial Proteins; D000244:Adenosine Diphosphate; D019731:Carbon-Nitrogen Ligases; C021557:5,10-methenyltetrahydrofolate synthetase; D008274:Magnesium