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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Sep;69(Pt 9):956-61. doi: 10.1107/S1744309113021246. Epub 2013 Aug 19.

Structure of isochorismate synthase DhbC from Bacillus anthracis.

Author information

1
Department of Molecular Physiology and Biological Physics, University of Virginia, 1340 Jefferson Park Avenue, Jordan Hall, Charlottesville, VA 22908, USA.

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.

KEYWORDS:

CSGID; DhbC; bacillibactin biosynthesis; isochorismate mutase; isochorismate synthase; siderophore biosynthesis

PMID:
23989140
PMCID:
PMC3758140
DOI:
10.1107/S1744309113021246
[Indexed for MEDLINE]
Free PMC Article

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