3OS6: Crystal Structure Of Putative 2,3-dihydroxybenzoate-specific Isochorismate Synthase, Dhbc From Bacillus Anthracis

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 A 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.
PDB ID: 3OS6Download
MMDB ID: 85661
PDB Deposition Date: 2010/9/8
Updated in MMDB: 2010/10
Experimental Method:
x-ray diffraction
Resolution: 2.4  Å
Source Organism:
Similar Structures:
Biological Unit for 3OS6: dimeric; determined by author and by software (PISA)
Molecular Components in 3OS6
Label Count Molecule
Proteins (2 molecules)
Isochorismate Synthase Dhbc
Molecule annotation
Chemicals (18 molecules)
* Click molecule labels to explore molecular sequence information.

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