Structural highlights
Function
Q8EBV3_SHEON
Publication Abstract from PubMed
Shewanella oneidensis, a Gram-negative gamma-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.
Structural 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 SN FEBS Lett. 2017 Sep 4. doi: 10.1002/1873-3468.12833. PMID:28869767[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Elegheert J, Brige A, Van Beeumen J, Savvides SN. Structural dissection of Shewanella oneidensis old yellow enzyme 4 bound to a Meisenheimer complex and (nitro)phenolic ligands. FEBS Lett. 2017 Sep 4. doi: 10.1002/1873-3468.12833. PMID:28869767 doi:http://dx.doi.org/10.1002/1873-3468.12833