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Fig. 4 | Biotechnology for Biofuels and Bioproducts

Fig. 4

From: Efficient production of salicylic acid through CmeR-PcmeO biosensor-assisted multiplexing pathway optimization in Escherichia coli

Fig. 4

Structural prediction and analysis of the regulator CmeR and the mutant CmeRF99A. a The CmeR protein is depicted in cyan. b The CmeRF99A protein is represented in blue. Homology modeling of CmeRF99A was performed using the CmeR protein template in Discovery Studio. Upon substitution of phenylalanine with alanine at position 99 (F99A), structural analysis revealed a distinct protrusion formation within the ligand-binding pocket. This conformational alteration significantly modified the interaction pattern between the mutant protein and SA, particularly in terms of binding orientation and potential contact residues

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