Ontology highlight
ABSTRACT:
SUBMITTER: Domagalski MJ
PROVIDER: S-EPMC3758140 | biostudies-literature | 2013 Sep
REPOSITORIES: biostudies-literature
Domagalski M J MJ Tkaczuk K L KL Chruszcz M M Skarina T T Onopriyenko O O Cymborowski M M Grabowski M M Savchenko A A Minor W W
Acta crystallographica. Section F, Structural biology and crystallization communications 20130819 Pt 9
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 t ...[more]