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. 2016 Dec 15;5:e20198. doi: 10.7554/eLife.20198

Figure 6. Ligand-binding sites in the CGP-TbAdoMetDC/prozyme heterodimer structure.

(A) Overlay of CGP-TbAdoMetDC β/α (teal/sky blue, CGP 40215 (TbCGP) and B3P in purple), prozyme (yellow, TbPut’ in orange) and HsAdoMetDC (3DZ6) β/α (dark green/light green, HsPut in green) structures viewed from the dimer interface. The schematic above the figure depicts color codes for the various chains. (B–C) Limited 4 Å shell showing the B3P- and putrescine-binding sites in TbAdoMetDC (B) and prozyme (C). (D) Overlay of the TbAdoMetDC CGP-binding site with HsAdoMetDC showing select residues in the 4 Å shell. H-bond interactions (distance < 3.3 Å) are shown by dashed lines. The electron density supporting ligand placement is shown in Figure 3—figure supplement 2, the complete structural alignment of Hs and Tb AdoMetDCs in Figure 6—figure supplement 1 and the comparison of the unliganded and liganded TbAdoMetDC structures in Figure 6—figure supplement 2.

DOI: http://dx.doi.org/10.7554/eLife.20198.016

Figure 6.

Figure 6—figure supplement 1. Comparison of TbAdoMetDC/prozyme and HsAdoMetDC dimer.

Figure 6—figure supplement 1.

Alignment of TbAdoMetDC/prozyme CGP 40215-bound heterodimer (AdoMetDC β/α (teal/sky blue), prozyme (yellow)) with HsAdoMetDC 1i7M (β/α (bright green/light green). TbAdoMetDC pyruvoyl (TbPvl 86) is shown as dots. HsAdoMetDC ligands AAH (lines) and putrescine (spheres) are shown in green, TbAdoMetDC ligands (CGP and B3P) are shown in purple and Put is shown in tan, as is prozyme Put'. AdoMetDC subunits aligned with an RMSD of 1.6 Å over 290 Cα atoms.
DOI: http://dx.doi.org/10.7554/eLife.20198.017
Figure 6—figure supplement 2. Comparison of apo- and CGP-bound TbAdoMetDC/prozyme active site.

Figure 6—figure supplement 2.

Alignment of the AdoMetDC/prozyme apo structure (tan) with the CGP-bound structure (β/α in teal/sky blue) showing the active site region.
DOI: http://dx.doi.org/10.7554/eLife.20198.018