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Bacterial signaling can occur within bacteria (intracellular) or between bacteria (intercellular). At times, a group of bacteria behaves like a community. To achieve this, they engage in quorum sensing, the perception of higher cell density that causes changes in gene expression. Quorum sensing involves both extracellular and intracellular signaling. The signaling cascade starts with a molecule called an autoinducer (AI). Individual bacteria produce AIs that move out of the bacterial cell...
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Structural basis for bacterial quorum sensing-mediated oxalogenesis.

Juntaek Oh1, Eunhye Goo1, Ingyu Hwang1

  • 1Department of Agricultural Biotechnology and Seoul National University, Seoul 151-921, Korea.

The Journal of Biological Chemistry
|March 12, 2014
PubMed
Summary

Burkholderia bacteria produce oxalic acid via ObcA enzyme during quorum sensing to survive. This study reveals ObcA

Keywords:
Acetyl Coenzyme ABacterial PathogenesisBurkholderia glumaeEnzyme CatalysisObcAOxalateOxalate Biosynthetic ComponentProtein StructureX-ray Crystallography

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Area of Science:

  • Biochemistry
  • Microbiology
  • Structural Biology

Background:

  • Burkholderia species produce oxalic acid, a public good essential for group survival.
  • Oxalogenesis is crucial for counteracting alkaline pH during bacterial stationary growth phase.
  • Quorum sensing regulates this vital metabolic process.

Purpose of the Study:

  • To elucidate the structural and functional mechanisms of ObcA, an enzyme involved in oxalogenesis.
  • To understand how ObcA differs mechanistically from citrate synthase.
  • To provide a structural basis for the first step of oxalogenesis.

Main Methods:

  • X-ray crystallography was used for structural analysis of ObcA.
  • Complexes of ObcA with oxaloacetate and a bisubstrate adduct were analyzed.
  • Functional assays were performed to determine the catalytic mechanism.

Main Results:

  • ObcA possesses a unique (β/α)8-barrel fold with an inserted N-domain.
  • Oxaloacetate and acetyl-CoA bind to distinct sites near the metal coordination shell.
  • Oxaloacetate forms an enolate intermediate, attacking acetyl-CoA to form a stable tetrahedral adduct.

Conclusions:

  • ObcA combines enolase and acetyltransferase activities with distinct features.
  • The enzyme's unique catalytic strategy facilitates survival and adaptation.
  • This study provides key insights into the mechanism of bacterial oxalogenesis.