3OS6
Crystal structure of putative 2,3-dihydroxybenzoate-specific isochorismate synthase, DhbC from Bacillus anthracis.
Summary for 3OS6
| Entry DOI | 10.2210/pdb3os6/pdb |
| Descriptor | Isochorismate synthase DhbC, SULFATE ION, POLYETHYLENE GLYCOL (N=34), ... (5 entities in total) |
| Functional Keywords | structural genomics, center for structural genomics of infectious diseases, csgid, isochorismate synthase dhbc, isomerase |
| Biological source | Bacillus anthracis (anthrax,anthrax bacterium) |
| Total number of polymer chains | 4 |
| Total formula weight | 186280.77 |
| Authors | Domagalski, M.J.,Chruszcz, M.,Skarina, T.,Onopriyenko, O.,Cymborowski, M.,Savchenko, A.,Edwards, A.,Anderson, W.,Minor, W.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2010-09-08, release date: 2010-10-20, Last modification date: 2024-11-06) |
| Primary citation | Domagalski, M.J.,Tkaczuk, K.L.,Chruszcz, M.,Skarina, T.,Onopriyenko, O.,Cymborowski, M.,Grabowski, M.,Savchenko, A.,Minor, W. Structure of isochorismate synthase DhbC from Bacillus anthracis. Acta Crystallogr.,Sect.F, 69:956-961, 2013 Cited by PubMed 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. PubMed: 23989140DOI: 10.1107/S1744309113021246 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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