7NDS

Crystal structure of TphC in a closed conformation

Summary for 7NDS

• Entry DOI: 10.2210/pdb7nds/pdb
• Descriptor: Tripartite tricarboxylate transporter substrate binding protein, terephthalic acid (3 entities in total)
• Functional Keywords: solute binding protein, transport protein
• Biological source: Comamonas sp.
• Total number of polymer chains: 1
• Total formula weight: 33958.84

Authors

Levy, C. (deposition date: 2021-02-02, release date: 2021-11-03, Last modification date: 2024-01-31)

Primary citation

Gautom, T.,Dheeman, D.,Levy, C.,Butterfield, T.,Alvarez Gonzalez, G.,Le Roy, P.,Caiger, L.,Fisher, K.,Johannissen, L.,Dixon, N.
Structural basis of terephthalate recognition by solute binding protein TphC.
Nat Commun, 12:6244-6244, 2021

PubMed 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.

PubMed: 34716322
DOI: 10.1038/s41467-021-26508-0

Experimental method

X-RAY DIFFRACTION (2.4 Å)