Fig. 4

Conformational Differences among Wild Type and Mutant Sedolisins. a Cartoon of the SED_A model with regions that have a resQ score below 5 Å in grey, homologous regions above 5 Å in orange and CSIs with resQ above 5 Å in red. b ResQ plot of SED_A modeling. c Schematic representation of the major structural differences in secondary structure elements of the polypeptide between helices 9 and 12 observed in WT and mutant models of SED_A and SED_B as compared to the 3EE6 structure. Quintuple refers to the virtual SED_A A343F-F92L-E404L-K407Q-L410S mutant. Yellow diamonds indicate conserved cysteines that are possibly involved in a novel disulfide bridge. Approximate positions of SDPs 307, 343, 346 and 349 are indicated from left to right by a green check mark. Absent counterparts are represented as a red cross. Helices are in red cyinders and sheets in blue arrows. d Local detail of the structural alignment of 3EE6 (blue cartoon) with model obtained for WT SED_B (cyan cartoon). The wireframe indicates the predicted binding cleft with the catalytic triade in red and the oxyanion in orange. e Local detail of the structural alignment of WT SED_A model (green cartoon) and the SED_A quintuple mutant model (yellow cartoon). The wireframe indicates the predicted binding cleft with the catalytic triade in red and the oxyanion in orange. Helix numbers are indicated in the 3EE6 structure