Fig. 5: Penicillamine (L-Pen) binding in the ThAOS active site. | Communications Chemistry

Fig. 5: Penicillamine (L-Pen) binding in the ThAOS active site.

From: Rational engineering of a thermostable α-oxoamine synthase biocatalyst expands the substrate scope and synthetic applicability

Fig. 5

A Experimental electron density map showing the PLP:L-Pen thiazolidine in the ThAOS V79A variant (PDB: 8S1Y). The two protein chains are coloured gold and blue, the side-chain from the other subunit is A79’, the ligand is shown with grey carbon atoms and the 2mFo-DFc map is shown as a blue transparent surface at a level of 1σ. B Comparison of the ThAOS wild-type structure with the V79A variant. The loss of the V79 side chain (shown in pink from the WT structure (PDB: 7POA)), does not cause any gross structural changes at the active site. Removal of V79 opens this region up by around 1 Å, to allow larger hydrophobic substrates to be accommodated. C The chemistry of the PLP:L-Pen external aldimine and ring closed PLP:L-Pen thiazolidine observed in the ThAOS V79A structure. Figure created using ChimeraX version 1.6.1.

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