Structural basis of terephthalate recognition by solute binding protein TphC

Trishnamoni Gautom, Dharmendra Dheeman, Colin Levy, Thomas Butterfield, Guadalupe Alvarez Gonzalez, Philip Roy, Lewis Caiger, Karl Fisher, Linus Johannissen and Neil Dixon ()
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Trishnamoni Gautom: The University of Manchester
Dharmendra Dheeman: The University of Manchester
Colin Levy: The University of Manchester
Thomas Butterfield: The University of Manchester
Guadalupe Alvarez Gonzalez: The University of Manchester
Philip Roy: The University of Manchester
Lewis Caiger: The University of Manchester
Karl Fisher: The University of Manchester
Linus Johannissen: The University of Manchester
Neil Dixon: The University of Manchester

Nature Communications, 2021, vol. 12, issue 1, 1-12

Abstract: 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.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-26508-0

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DOI: 10.1038/s41467-021-26508-0

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