7QFX

Crystal structure of Old Yellow Enzyme AnOYE8 from Aspergillus niger

Summary for 7QFX

• Entry DOI: 10.2210/pdb7qfx/pdb
• Descriptor: NADH-dependent flavin oxidoreductase, SULFATE ION, FLAVIN MONONUCLEOTIDE, ... (5 entities in total)
• Functional Keywords: old yellow enzyme, ene-reductase, oxidoreductase
• Biological source: Aspergillus niger
• Total number of polymer chains: 4
• Total formula weight: 185967.80

Authors

Robescu, M.S.,Loprete, G.,Vascon, F.,Gasparotto, M.,Filippini, F.,Bergantino, E.,Cendron, L. (deposition date: 2021-12-06, release date: 2022-04-20, Last modification date: 2024-02-07)

Primary citation

Robescu, M.S.,Loprete, G.,Gasparotto, M.,Vascon, F.,Filippini, F.,Cendron, L.,Bergantino, E.
The Family Keeps on Growing: Four Novel Fungal OYEs Characterized.
Int J Mol Sci, 23:-, 2022

PubMed Abstract: Aiming at expanding the portfolio of Old Yellow Enzymes (OYEs), which have been systematically studied to be employed in the chemical and pharmaceutical industries as useful biocatalysts, we decided to explore the immense reservoir of filamentous fungi. We drew from the genome of the two Ascomycetes and four new members of the OYE superfamily belonging to the classical and thermophilic-like subfamilies. The two OYEs show wider substrate spectra than the OYE homologues, which appear as more specialized biocatalysts. According to their mesophilic origins, the new enzymes neither show high thermostability nor extreme pH optimums. The crystal structures of OYE4 and OYE8 have been determined, revealing the conserved features of the thermophilic-like subclass as well as unique properties, such as a peculiar N-terminal loop involved in dimer surface interactions. For the classical representatives OYE1 and OYE2, model structures were built and analyzed, showing surprisingly wide open access to the active site cavities due to a shorter β6-loop and a disordered capping subdomain.

PubMed: 35328465
DOI: 10.3390/ijms23063050

Experimental method

X-RAY DIFFRACTION (2.8 Å)