Structural basis of terephthalate recognition by solute binding protein TphC

Nat Commun. 2021 Oct 29;12(1):6244. doi: 10.1038/s41467-021-26508-0.

Abstract

Biological degradation of Polyethylene terephthalate (PET) plastic and assimilation of the corresponding monomers ethylene glycol and terephthalate (TPA) into central metabolism offers an attractive route for bio-based molecular recycling and bioremediation applications. A key step is the cellular uptake of the non-permeable TPA into bacterial cells which has been shown to be dependent upon the presence of the key tphC gene. However, little is known from a biochemical and structural perspective about the encoded solute binding protein, TphC. Here, we report the biochemical and structural characterisation of TphC in both open and TPA-bound closed conformations. This analysis demonstrates the narrow ligand specificity of TphC towards aromatic para-substituted dicarboxylates, such as TPA and closely related analogues. Further phylogenetic and genomic context analysis of the tph genes reveals homologous operons as a genetic resource for future biotechnological and metabolic engineering efforts towards circular plastic bio-economy solutions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism*
  • Calorimetry
  • Comamonas / chemistry
  • Comamonas / genetics*
  • Comamonas / metabolism
  • Crystallography, X-Ray
  • Fluorometry / methods
  • Ligands
  • Models, Molecular
  • Molecular Docking Simulation
  • Mutation
  • Operon
  • Phthalic Acids / metabolism*
  • Phylogeny
  • Protein Conformation
  • Xenobiotics / metabolism

Substances

  • Bacterial Proteins
  • Ligands
  • Phthalic Acids
  • Xenobiotics
  • terephthalic acid