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Fig. 5 | Biotechnology for Biofuels

Fig. 5

From: An iterative computational design approach to increase the thermal endurance of a mesophilic enzyme

Fig. 5

Mutations in PDC2.03 imparting an increase in thermal stability and endurance without changing the backbone. a The Cα atoms at mutated positions are highlighted as spheres. The mutations that comprise PDC2.03 are located throughout the PDC enzyme. Mutations from PDC1.01 are shown in yellow, PDC1.10 in blue, and the mutations added to generate PDC2.03 are shown in red. Chains A and E are shown in dark gray, and chains B and F are shown in light gray, respectively. b The mutations in PDC2.03 are found in each of the three structural regions of PDC monomer. c The X-ray crystal structure of PDC2.03 (PDB code 5TMA) is shown in purple aligned with the wild-type PDC in gray (PDB code 2WVA). The Cα backbone root-mean-square deviation (RMSD) for the PDC monomeric unit is 0.19 Å

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