Skip to main content
. Author manuscript; available in PMC: 2017 Jun 5.
Published in final edited form as: Enzymes. 2016 Mar 28;39:293–323. doi: 10.1016/bs.enz.2016.02.002

Fig. 1.

Fig. 1

Universal and adapted features of polymerase structures. (A) PV RdRp structure. Conserved structural motifs in the palm subdomain are colored as follows: motif A, red (dark gray in the print version); motif B, green (dark gray in the print version); motif C, yellow (light gray in the print version); motif D, blue (dark gray in the print version); motif E, purple (gray in the print version); motif F, orange (gray in the print version); and motif G, black. (B) The NTP-binding site. The “universal” interactions are observed in all polymerases. The “adapted” interactions dictate the sugar configuration recognized by the polymerase. Reprinted with permission from D.W. Gohara, J.J. Arnold, C.E. Cameron, Poliovirus RNA-dependent RNA polymerase (3Dpol): kinetic, thermodynamic, and structural analysis of ribonucleotide selection, Biochemistry 43 (18) (2004) 5149–5158. Copyright (2004) American Chemical Society.