6ZE7
Chaetomium thermophilum FAD-dependent oxidoreductase in complex with 4-nitrophenol
Summary for 6ZE7
| Entry DOI | 10.2210/pdb6ze7/pdb |
| Related | 6ZE2 6ZE3 6ZE4 6ZE5 6ZE6 7AA2 |
| Descriptor | FAD-dependent oxidoreductase, MAGNESIUM ION, SODIUM ION, ... (12 entities in total) |
| Functional Keywords | chaetomium thermophilum, glucose-methanol-choline oxidoreductase, 4-nitrophenol, co-crystallization, oxidoreductase |
| Biological source | Chaetomium thermophilum var. thermophilum DSM 1495 |
| Total number of polymer chains | 2 |
| Total formula weight | 134022.57 |
| Authors | Svecova, L.,Skalova, T.,Kolenko, P.,Koval, T.,Oestergaard, L.H.,Dohnalek, J. (deposition date: 2020-06-16, release date: 2021-05-26, Last modification date: 2024-11-13) |
| Primary citation | Svecova, L.,Ostergaard, L.H.,Skalova, T.,Schnorr, K.M.,Koval', T.,Kolenko, P.,Stransky, J.,Sedlak, D.,Duskova, J.,Trundova, M.,Hasek, J.,Dohnalek, J. Crystallographic fragment screening-based study of a novel FAD-dependent oxidoreductase from Chaetomium thermophilum. Acta Crystallogr D Struct Biol, 77:755-775, 2021 Cited by PubMed Abstract: The FAD-dependent oxidoreductase from Chaetomium thermophilum (CtFDO) is a novel thermostable glycoprotein from the glucose-methanol-choline (GMC) oxidoreductase superfamily. However, CtFDO shows no activity toward the typical substrates of the family and high-throughput screening with around 1000 compounds did not yield any strongly reacting substrate. Therefore, protein crystallography, including crystallographic fragment screening, with 42 fragments and 37 other compounds was used to describe the ligand-binding sites of CtFDO and to characterize the nature of its substrate. The structure of CtFDO reveals an unusually wide-open solvent-accessible active-site pocket with a unique His-Ser amino-acid pair putatively involved in enzyme catalysis. A series of six crystal structures of CtFDO complexes revealed five different subsites for the binding of aryl moieties inside the active-site pocket and conformational flexibility of the interacting amino acids when adapting to a particular ligand. The protein is capable of binding complex polyaromatic substrates of molecular weight greater than 500 Da. PubMed: 34076590DOI: 10.1107/S2059798321003533 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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