4B5N

Crystal structure of oxidized Shewanella Yellow Enzyme 4 (SYE4)

Summary for 4B5N

• Entry DOI: 10.2210/pdb4b5n/pdb
• Descriptor: OXIDOREDUCTASE, FMN-BINDING, FLAVIN MONONUCLEOTIDE, Octadecane, ... (4 entities in total)
• Functional Keywords: oxidoreductase, cofactor-binding
• Biological source: SHEWANELLA ONEIDENSIS MR-1
• Total number of polymer chains: 1
• Total formula weight: 39839.88

Authors

Elegheert, J.,Brige, A.,Savvides, S.N. (deposition date: 2012-08-07, release date: 2013-08-21, Last modification date: 2023-12-20)

Primary citation

Elegheert, J.,Brige, A.,Van Beeumen, J.,Savvides, S.N.
Structural dissection of Shewanella oneidensis old yellow enzyme 4 bound to a Meisenheimer complex and (nitro)phenolic ligands.
FEBS Lett., 591:3391-3401, 2017

PubMed Abstract: Shewanella oneidensis, a Gram-negative γ-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.

PubMed: 28869767
DOI: 10.1002/1873-3468.12833

Experimental method

X-RAY DIFFRACTION (1.1 Å)