Skip to main content
. 2016 Sep 29;2(10):702–709. doi: 10.1021/acscentsci.6b00184

Figure 6.

Figure 6

Docking model of LarA and LarB1. Model manually generated using FoldIt with homology models, BLI data, and cross-linking data as distance restraints. AzF constructs analyzed are shown in red, and corresponding regions of cross-linking are shown in orange. LarB1 is shown in green, LarA leader peptide residues 8–26 are shown in magenta, and LarA core peptide residues 27–35 are shown in cyan. (A) LarB1 homology model after LarA docking (LarA hidden). Note the shift of the β1 and β2 strands as compared to the homology model before docking (Figure 5C). (B) Predicted interaction from bioinformatics analysis between LarA Y10 (dark gray) and LarB1 D69 (light gray); LarA F21Z cross-linked to LarB1 Y28. (C) LarB1 Y28Z cross-linked to the Y32–R33 region of LarA. (D) LarB1 Q30Z cross-linked to the Q29–R33 region of LarA. (E) LarB1 Y16Z and LarB1 V19Z both cross-linked to the T24–A26 region of LarA. The LarB1 V19Z restraint could not be satisfied, likely because substitution of V19, a buried hydrophobic residue, with the larger AzF caused a structural change to LarB1. (F) LarA W35Z cross-linked to two regions, LarB1 Y16 and LarB1 A35–A36, that are far apart in amino acid sequence but close together in space.