Structure of isochorismate synthase DhbC from Bacillus anthracis. Issue 9 (30th August 2013)

• Record Type: Journal Article
• Authors: Domagalski, M. J.; Tkaczuk, K. L.; Chruszcz, M.; Skarina, T.; Onopriyenko, O.; Cymborowski, M.; Grabowski, M.; Savchenko, A.; Minor, W.
• Is Part Of: Acta crystallographica. Volume 69:Issue 9(2013:Sep.)
• Page Start: 956
• Page End: 961
• Publication Date: 2013-08-30
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113021246
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The isochorismate synthase DhbC from <italic>Bacillus anthracis</italic> 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. <italic>B. anthracis</italic> DhbC bears the strongest resemblance to the <italic>Escherichia coli</italic> 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 Mg²⁺‐dependent catalytic mechanism.</p> </abstract>