Figure 1 | Scientific Reports

Figure 1

From: The role of local and remote amino acid substitutions for optimizing fluorescence in bacteriophytochromes: A case study on iRFP

Figure 1

Top, structure of the chromophore binding pocket of P2PG (left) and iRFP (right), indicating the amino acid variations between both variants.

The structural models18 were derived from the crystal structure of the chromophore binding domain of RpBphP2 obtained by homologue-directed mutagenesis, which was termed RpBphP2-CBD* 29. Bottom, schematic presentation of the step-wise amino acid substitutions starting from P2PG WT (route A) and from iRFP (route B).

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