4C0X
The crystal strucuture of PpAzoR in complex with anthraquinone-2- sulfonate
Summary for 4C0X
| Entry DOI | 10.2210/pdb4c0x/pdb |
| Descriptor | FMN-DEPENDENT NADH-AZOREDUCTASE 1, FLAVIN MONONUCLEOTIDE, 9,10-dioxo-9,10-dihydroanthracene-2-sulfonic acid, ... (6 entities in total) |
| Functional Keywords | oxidoreductase, azoreductase, nad(p)h quinone oxidoreductase |
| Biological source | PSEUDOMONAS PUTIDA |
| Total number of polymer chains | 1 |
| Total formula weight | 22731.42 |
| Authors | Goncalves, A.M.D.,de Sanctis, D.,Bento, I. (deposition date: 2013-08-08, release date: 2013-10-30, Last modification date: 2023-12-20) |
| Primary citation | Goncalves, A.M.D.,Mendes, S.,De Sanctis, D.,Martins, L.O.,Bento, I. The Crystal Structure of Pseudomonas Putida Azor: The Active Site Revisited. FEBS J., 280:6643-, 2013 Cited by PubMed Abstract: The enzymatic degradation of azo dyes begins with the reduction of the azo bond. In this article, we report the crystal structures of the native azoreductase from Pseudomonas putida MET94 (PpAzoR) (1.60 Å), of PpAzoR in complex with anthraquinone-2-sulfonate (1.50 Å), and of PpAzoR in complex with Reactive Black 5 dye (1.90 Å). These structures reveal the residues and subtle changes that accompany substrate binding and release. Such changes highlight the fine control of access to the catalytic site that is required by the ping-pong mechanism, and in turn the specificity offered by the enzyme towards different substrates. The topology surrounding the active site shows novel features of substrate recognition and binding that help to explain and differentiate the substrate specificity observed among different bacterial azoreductases. PubMed: 24127652DOI: 10.1111/FEBS.12568 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.499 Å) |
Structure validation
Download full validation report
