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Structural dissection of Shewanella oneidensis old yellow enzyme 4 bound to a Meisenheimer complex and (nitro)phenolic ligands.

Jonathan ElegheertAnn BrigéJozef Van BeeumenSavvas N Savvides
Published in: FEBS letters (2017)
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.
Keyphrases
  • amino acid
  • gram negative
  • high resolution
  • oxidative stress
  • multidrug resistant
  • dna binding
  • mass spectrometry
  • ionic liquid
  • high throughput
  • transcription factor
  • high speed
  • heat shock
  • diabetic rats
  • electron transfer