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. 2022 Sep 6;119(37):e2123092119. doi: 10.1073/pnas.2123092119

Fig. 4.

Fig. 4.

Interactions between Dgt, Gp1.2, and dGTP. Middle, overview of the Dgt–Gp1.2–dGTP structure. Dgt and Gp1.2 are colored by monomer, while the dGTPs are colored green. Top Left, close-up of hydrogen-bond interactions between Gp1.2 and Dgt monomer A. Bottom Left, close-up of cation–π interactions between Gp1.2 and Dgt monomer E. The apo-Dgt (PDB ID: 4XDS, colored salmon) is aligned by the monomer A active-site histidine-aspartate (HD) motif. A portion of monomer E is displaced by >4 Å (as measured by the R436E C-α) to accommodate Gp1.2 helix α1. Top Right, close-up of interactions between Gp1.2, Dgt monomer A, and dGTP. Bottom Right, point of view rotated ∼90° from the image in the Top Right. The Middle images were generated in ChimeraX, while the other images were generated in Chimera.