title: Structure of isochorismate synthase DhbC from Bacillus anthracis.
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.
authors.affiliation: Department of Molecular Physiology and Biological Physics, University of Virginia, 1340 Jefferson Park Avenue, Jordan Hall, Charlottesville, VA 22908, USA.
authors.forename: M J
authors.initials: MJ
authors.lastname: Domagalski
authors.forename: K L
authors.initials: KL
authors.lastname: Tkaczuk
authors.forename: M
authors.initials: M
authors.lastname: Chruszcz
authors.forename: T
authors.initials: T
authors.lastname: Skarina
authors.forename: O
authors.initials: O
authors.lastname: Onopriyenko
authors.forename: M
authors.initials: M
authors.lastname: Cymborowski
authors.forename: M
authors.initials: M
authors.lastname: Grabowski
authors.forename: A
authors.initials: A
authors.lastname: Savchenko
authors.forename: W
authors.initials: W
authors.lastname: Minor
mesh_terms: D000595:Amino Acid Sequence; D001408:Bacillus anthracis / Q000737:chemistry* / Q000201:enzymology / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D020134:Catalytic Domain; D002413:Cations, Divalent; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D004758:Enterobactin / Q000096:biosynthesis / Q000737:chemistry; D004926:Escherichia coli / Q000737:chemistry / Q000201:enzymology / Q000235:genetics; D019751:Intramolecular Transferases / Q000737:chemistry* / Q000378:metabolism; D008274:Magnesium / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000096:biosynthesis / Q000737:chemistry*; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012645:Selenomethionine / Q000737:chemistry / Q000378:metabolism; D017262:Siderophores / Q000096:biosynthesis / Q000737:chemistry*; D040681:Structural Homology, Protein
chemical_list: D001426:Bacterial Proteins; D002413:Cations, Divalent; D009842:Oligopeptides; D011994:Recombinant Proteins; D017262:Siderophores; C430721:bacillibactin; D004758:Enterobactin; D012645:Selenomethionine; D019751:Intramolecular Transferases; C058486:isochorismate synthase; D008274:Magnesium
keywords: CSGID; DhbC; bacillibactin biosynthesis; isochorismate mutase; isochorismate synthase; siderophore biosynthesis