Published in
International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 9(69), p. 956-961
DOI: 10.1107/s1744309113021246
Links
- ORCID
- ORCID
- ORCID
- International Union of Crystallography
- [www.ncbi.nlm.nih.gov] | PDF
- [europepmc.org] | PDF
- [www.researchgate.net] | PDF
- [www.ncbi.nlm.nih.gov] | PDF
Tools
Structure of isochorismate synthase DhbC fromBacillus anthracis
,
K. L. Tkaczuk,
M. Chruszcz ,
T. Skarina,
O. Onopriyenko,
M. Cymborowski,
M. Grabowski,
A. Savchenko,
W. Minor
Full text: Download
Abstract
The isochorismate synthase DhbC from Bacillus anthracis is essential for the biosynthesis of the siderophore bacillibactin by this pathogenic bacterium. The structure of the selenomethionine-substituted protein was determined to 2.4 Å resolution using single-wavelength anomalous diffraction. B. anthracis DhbC bears the strongest resemblance to the Escherichia coli isochorismate synthase EntC, which is involved in the biosynthesis of another siderophore, namely enterobactin. Both proteins adopt the characteristic fold of other chorismate-utilizing enzymes, which are involved in the biosynthesis of various products, including siderophores, menaquinone and tryptophan. The conservation of the active-site residues, as well as their spatial arrangement, suggests that these enzymes share a common Mg(2+)-dependent catalytic mechanism.