Fig. 6
From: A novel hydroxycinnamoyl transferase for synthesis of hydroxycinnamoyl spermine conjugates in plants
Spatial interaction of spermine/spermidine and SrSpmHT/SrSHT. a, The 3D structure of SrSpmHT and SrSHT. Substrate binding pocket was marked with dotted yellow cycle. b, Comparison of the best docking results of spermidine and spermine in SrSHT or SrSpmHT active site. SrSHT or SrSpmHT structure is depicted in ribbon representation. For SrSHT, the N-terminal domain (residues 1–191) is colored in orange red and the C-terminal domain (residues 227–449) is colored in blue. The conserved and catalytic residues His156 is shown in side chain/base. The large crossover loop (amino acids 191-227) that connects both domains is marked in green. For SrSpmSHT, the N-terminal domain (residues 6–199) is colored in hot pink and the C-terminal domain (residues 223–447) is colored in cyan. The conserved and catalytic residues His160 is shown in side chain/base. The large crossover loop (amino acids 199-223) that connects both domains is marked in green. The spermidine is represented as a blue and stick model, and the spermine is represented as a pink and stick model. Visualization is performed using UCSF Chimera