8PUN
Old Yellow Enzyme from the thermophilic Ferrovum sp. JA12
Summary for 8PUN
| Entry DOI | 10.2210/pdb8pun/pdb |
| Descriptor | NADPH dehydrogenase, FLAVIN MONONUCLEOTIDE, DI(HYDROXYETHYL)ETHER, ... (10 entities in total) |
| Functional Keywords | oye, thermophilic, ene-reductase, fmn, flavoenzyme, oxidoreductase |
| Biological source | Ferrovum sp. JA12 |
| Total number of polymer chains | 4 |
| Total formula weight | 166829.30 |
| Authors | Polidori, N.,Gruber, K. (deposition date: 2023-07-17, release date: 2023-08-02, Last modification date: 2025-05-14) |
| Primary citation | Polidori, N.,Babin, P.,Daniel, B.,Gruber, K. Structure, Oligomerization, and Thermal Stability of a Recently Discovered Old Yellow Enzyme. Proteins, 93:1181-1188, 2025 Cited by PubMed Abstract: The Old Yellow Enzyme from Ferrovum sp. JA12 (FOYE) displays an unusual thermal stability for an enzyme isolated from a mesophilic organism. We determined the crystal structure of this enzyme and performed bioinformatic characterization to get insights into its thermal stability. The enzyme displays a tetrameric quaternary structure; however, unlike the other tetrameric homologs, it clusters in a separate phylogenetic group and possesses unique interactions that stabilize this oligomeric state. The thermal stability of this enzyme is mainly due to an unusually high number of intramolecular hydrogen bonds. Finally, this study provides a general analysis of the forces driving the oligomerization in Old Yellow Enzymes. PubMed: 39840754DOI: 10.1002/prot.26800 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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