The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding
oleh: Nicolas Tarbouriech, Corinne Ducournau, Stephanie Hutin, Philippe J. Mas, Petr Man, Eric Forest, Darren J. Hart, Christophe N. Peyrefitte, Wim P. Burmeister, Frédéric Iseni
| Format: | Article |
|---|---|
| Diterbitkan: | Nature Portfolio 2017-11-01 |
Deskripsi
The catalytic subunit E9 of the vaccinia virus DNA polymerase forms a functional polymerase holoenzyme by interacting with the heterodimeric processivity factor A20/D4. Here the authors present the structure of full-length E9 and show that an insertion within its palm domain binds A20, in a mode different from other family B polymerases.