8CCQ
Crystal structure of arsenite oxidase from Pseudorhizobium banfieldiae str. NT-26 (NT-26 Aio) bound to antimony trioxide
Summary for 8CCQ
| Entry DOI | 10.2210/pdb8ccq/pdb |
| Descriptor | AroA, TRIHYDROXYANTIMONITE(III), 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL, ... (13 entities in total) |
| Functional Keywords | arsenite oxidase, molybdenum cofactor, mgd, arsenic oxyanion, antimony oxyanion, oxidoreductase |
| Biological source | Pseudorhizobium banfieldiae More |
| Total number of polymer chains | 8 |
| Total formula weight | 459317.70 |
| Authors | Engrola, F.,Santos-Silva, T.,Romao, M.J.,Correia, M.A.S. (deposition date: 2023-01-27, release date: 2023-07-12, Last modification date: 2023-09-06) |
| Primary citation | Engrola, F.,Correia, M.A.S.,Watson, C.,Romao, C.C.,Veiros, L.F.,Romao, M.J.,Santos-Silva, T.,Santini, J.M. Arsenite oxidase in complex with antimonite and arsenite oxyanions: Insights into the catalytic mechanism. J.Biol.Chem., 299:105036-105036, 2023 Cited by PubMed Abstract: Arsenic contamination of groundwater is among one of the biggest health threats affecting millions of people in the world. There is an urgent need for efficient arsenic biosensors where the use of arsenic metabolizing enzymes can be explored. In this work, we have solved four crystal structures of arsenite oxidase (Aio) in complex with arsenic and antimony oxyanions and the structures determined correspond to intermediate states of the enzymatic mechanism. These structural data were complemented with density-functional theory calculations providing a unique view of the molybdenum active site at different time points that, together with mutagenesis data, enabled to clarify the enzymatic mechanism and the molecular determinants for the oxidation of As(III) to the less toxic As(V) species. PubMed: 37442232DOI: 10.1016/j.jbc.2023.105036 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.89 Å) |
Structure validation
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