Fig. 2: Active-site geometry of the Prim–PolC–DNA ternary complex.
From: Molecular basis for DNA repair synthesis on short gaps by mycobacterial Primase-Polymerase C
Molecular details of the docking of the 3′-terminal nucleotide of the incoming primer strand as the enzyme positions the 3′-OH moiety to attack the α-phosphate of the bound non-hydrolysable UTP analogue, UpNHpp. Hydrogen bonds are depicted in black, and dative bonding of the catalytic manganese ions (magenta spheres) is depicted in red. R179 appears to act as a gating side chain and is evidently in a closed position.
