Fig. 3: Structural comparison of the hPOLγ and mPolγ replication conformers.
From: Modelling POLG mutations in mice unravels a critical role of POLγΒ in regulating phenotypic severity
a Schematic overview of the domains in hPOLγA with the positions of the four disease variants marked, and the corresponding residues in mPolγA in parentheses. b Overview of overlaid hPOLγ (PDB ID: 8D37) and mPolγ replication conformers. The positions of the subunits; hPOLγA (magenta) and the hPOLγB dimer (white), are near identical to their mouse counterparts; mPolγA (green), proximal mPolγB (yellow) and distal mPolγB (blue). In both structures, the DNA is also in the same position. The DNA is colored gray (human) or beige (mouse). c Closeup of the catalytic site (POL) and the Y955/Y933 residues. The incoming nucleotide (dCTP) is highlighted in yellow. d Closeup of the A467/A449 position and surrounding residues. e Closeup of the W748/W726 position and surrounding residues. f Closeup of the G848/G826 position and surrounding residues. In c–f, the surrounding residues are numbered according to the human sequence.
