Download MendeleyStructural dissection of Shewanella oneidensis old yellow enzyme 4 bound to a Meisenheimer complex and (nitro)phenolic ligands.
Elegheert, J., Brige, A., Van Beeumen, J., Savvides, S.N.(2017) FEBS Lett 591: 3391-3401
- PubMed: 28869767
- DOI: https://doi.org/10.1002/1873-3468.12833
- Primary Citation of Related Structures:
4B5N, 5K0R, 5K1K, 5K1M, 5K1Q, 5K1U, 5K1W - PubMed Abstract:
Shewanella oneidensis, a Gram-negative ¦Ă-proteobacterium with an extensive redox capacity, possesses four old yellow enzyme (OYE) homologs. Of these, Shewanella yellow enzyme 4 (SYE4) is implicated in resistance to oxidative stress. Here, we present a series of high-resolution crystal structures for SYE4 in the oxidized and reduced states, and in complex with phenolic ligands and the nitro-aromatic explosive picric acid. The structures unmask new features, including the identification of a binding platform for long-chain hydrophobic molecules. Furthermore, we present the first structural observation of a hydride-Meisenheimer complex of picric acid with a flavoenzyme. Overall, our study exposes the binding promiscuity of SYE4 toward a variety of electrophilic substrates and is consistent with a general detoxification function for SYE4.
Organizational Affiliation:
Laboratory for Protein Biochemistry and Biomolecular Engineering (L-ProBE), Department of Biochemistry and Microbiology, Ghent University, Belgium.
