5TTK
Crystal Structure of Selenomethionine-incorporated Nicotine Oxidoreductase from Pseudomonas putida
Summary for 5TTK
| Entry DOI | 10.2210/pdb5ttk/pdb |
| Related | 5TTJ |
| Descriptor | Amine oxidase, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | nicotine degradation, flavoenzyme, monoamine oxidase family, phbh, oxidoreductase |
| Biological source | Pseudomonas putida (strain S16) |
| Total number of polymer chains | 4 |
| Total formula weight | 219679.56 |
| Authors | Tararina, M.A.,Janda, K.D.,Allen, K.N. (deposition date: 2016-11-03, release date: 2017-01-25, Last modification date: 2024-11-20) |
| Primary citation | Tararina, M.A.,Janda, K.D.,Allen, K.N. Structural Analysis Provides Mechanistic Insight into Nicotine Oxidoreductase from Pseudomonas putida. Biochemistry, 55:6595-6598, 2016 Cited by PubMed Abstract: The first structure of nicotine oxidoreductase (NicA2) was determined by X-ray crystallography. Pseudomonas putida has evolved nicotine-degrading activity to provide a source of carbon and nitrogen. The structure establishes NicA2 as a member of the monoamine oxidase family. Residues 1-50 are disordered and may play a role in localization. The nicotine-binding site proximal to the isoalloxazine ring of flavin shows an unusual composition of the classical aromatic cage (W427 and N462). The active site architecture is consistent with the proposed binding of the deprotonated form of the substrate and the flavin-dependent oxidation of the pyrrolidone C-N bond followed by nonenzymatic hydrolysis. PubMed: 27933790DOI: 10.1021/acs.biochem.6b00963 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.51 Å) |
Structure validation
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