2OQW
The crystal structure of sortase B from B.anthracis in complex with AAEK1
Summary for 2OQW
| Entry DOI | 10.2210/pdb2oqw/pdb |
| Descriptor | Sortase B (2 entities in total) |
| Functional Keywords | sortaseb protein, inhibitor, b. anthracis, the great lakes regional center of excellence, glrce, hydrolase |
| Biological source | Bacillus anthracis str. |
| Total number of polymer chains | 1 |
| Total formula weight | 26928.53 |
| Authors | Wu, R.,Zhang, R.,Marresso, A.W.,Schneewind, O.,Joachimiak, A. (deposition date: 2007-02-01, release date: 2007-06-19, Last modification date: 2023-12-27) |
| Primary citation | Maresso, A.W.,Wu, R.,Kern, J.W.,Zhang, R.,Janik, D.,Missiakas, D.M.,Duban, M.E.,Joachimiak, A.,Schneewind, O. Activation of inhibitors by sortase triggers irreversible modification of the active site. J.Biol.Chem., 282:23129-23139, 2007 Cited by PubMed Abstract: Sortases anchor surface proteins to the cell wall of Gram-positive pathogens through recognition of specific motif sequences. Loss of sortase leads to large reductions in virulence, which identifies sortase as a target for the development of antibacterials. By screening 135,625 small molecules for inhibition, we report here that aryl (beta-amino)ethyl ketones inhibit sortase enzymes from staphylococci and bacilli. Inhibition of sortases occurs through an irreversible, covalent modification of their active site cysteine. Sortases specifically activate this class of molecules via beta-elimination, generating a reactive olefin intermediate that covalently modifies the cysteine thiol. Analysis of the three-dimensional structure of Bacillus anthracis sortase B with and without inhibitor provides insights into the mechanism of inhibition and reveals binding pockets that can be exploited for drug discovery. PubMed: 17545669DOI: 10.1074/jbc.M701857200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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