8RNK
Unspecific peroxygenase from Marasmius wettsteinii (MweUPO-1) in complex with myristic acid
Summary for 8RNK
| Entry DOI | 10.2210/pdb8rnk/pdb |
| Related | 8RNJ |
| Descriptor | Unspecific peroxygenase, 2-acetamido-2-deoxy-beta-D-glucopyranose, MYRISTIC ACID, ... (9 entities in total) |
| Functional Keywords | peroxygenase, peroxidase, complex, myristic acid, oxidoreductase |
| Biological source | Marasmius wettsteinii |
| Total number of polymer chains | 2 |
| Total formula weight | 55515.32 |
| Authors | Fernandez-Garcia, A.,Sanz-Aparicio, J. (deposition date: 2024-01-10, release date: 2024-10-16, Last modification date: 2024-10-30) |
| Primary citation | Sanchez-Moreno, I.,Fernandez-Garcia, A.,Mateljak, I.,Gomez de Santos, P.,Hofrichter, M.,Kellner, H.,Sanz-Aparicio, J.,Alcalde, M. Structural Insights and Reaction Profile of a New Unspecific Peroxygenase from Marasmius wettsteinii Produced in a Tandem-Yeast Expression System. Acs Chem.Biol., 19:2240-2253, 2024 Cited by PubMed Abstract: Fungal unspecific peroxygenases (UPOs) are gaining momentum in synthetic chemistry. Of special interest is the UPO from (UPO), which shows an exclusive repertoire of oxyfunctionalizations, including the terminal hydroxylation of alkanes, the α-oxidation of fatty acids and the C-C cleavage of corticosteroids. However, the lack of heterologous expression systems to perform directed evolution has impeded its engineering for practical applications. Here, we introduce a close ortholog of UPO, a UPO gene from (UPO-1), that has a similar reaction profile to UPO and for which we have set up a directed evolution platform based on tandem-yeast expression. Recombinant UPO-1 was produced at high titers in the bioreactor (0.7 g/L) and characterized at the biochemical and atomic levels. The conjunction of soaking crystallographic experiments at a resolution up to 1.6 Å together with the analysis of reaction patterns sheds light on the substrate preferences of this promiscuous biocatalyst. PubMed: 39367827DOI: 10.1021/acschembio.4c00504 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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