7YNH
Catalytic intermediate of copper amine oxidase determined by serial femtosecond X-ray crystallography using a single-flow liquid jet system
Summary for 7YNH
| Entry DOI | 10.2210/pdb7ynh/pdb |
| Descriptor | Phenylethylamine oxidase, SODIUM ION, PHENYLACETALDEHYDE, ... (5 entities in total) |
| Functional Keywords | topaquinone, copper amine oxidase, serial femtosecond x-ray crystallography, oxidoreductase |
| Biological source | Arthrobacter globiformis |
| Total number of polymer chains | 2 |
| Total formula weight | 138240.87 |
| Authors | Murakawa, T.,Okajima, T. (deposition date: 2022-07-31, release date: 2022-11-16, Last modification date: 2024-11-13) |
| Primary citation | Murakawa, T.,Suzuki, M.,Fukui, K.,Masuda, T.,Sugahara, M.,Tono, K.,Tanaka, T.,Iwata, S.,Nango, E.,Yano, T.,Tanizawa, K.,Okajima, T. Serial femtosecond X-ray crystallography of an anaerobically formed catalytic intermediate of copper amine oxidase. Acta Crystallogr D Struct Biol, 78:1428-1438, 2022 Cited by PubMed Abstract: The mechanisms by which enzymes promote catalytic reactions efficiently through their structural changes remain to be fully elucidated. Recent progress in serial femtosecond X-ray crystallography (SFX) using X-ray free-electron lasers (XFELs) has made it possible to address these issues. In particular, mix-and-inject serial crystallography (MISC) is promising for the direct observation of structural changes associated with ongoing enzymic reactions. In this study, SFX measurements using a liquid-jet system were performed on microcrystals of bacterial copper amine oxidase anaerobically premixed with a substrate amine solution. The structure determined at 1.94 Å resolution indicated that the peptidyl quinone cofactor is in equilibrium between the aminoresorcinol and semiquinone radical intermediates, which accumulate only under anaerobic single-turnover conditions. These results show that anaerobic conditions were well maintained throughout the liquid-jet SFX measurements, preventing the catalytic intermediates from reacting with dioxygen. These results also provide a necessary framework for performing time-resolved MISC to study enzymic reaction mechanisms under anaerobic conditions. PubMed: 36458614DOI: 10.1107/S2059798322010385 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.94 Å) |
Structure validation
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