Open AccessStructure of 5‐formyltetrahydrofolate cyclo‐ligase from Bacillus anthracis (BA4489)
Author(s) -
Meier Christoph,
Carter Lester G.,
Winter Graeme,
Owens Ray J.,
Stuart David I.,
Esnouf Robert M.
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107007221
Subject(s) - bacillus anthracis , dna ligase , chemistry , enzyme , ubiquitin ligase , bacteria , bacillus (shape) , active site , biochemistry , computational biology , microbiology and biotechnology , biology , gene , ubiquitin , genetics
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 Å 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.