Bibliographic Details
| Title: |
The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding |
| Authors: |
Nicolas Tarbouriech, Corinne Ducournau, Stephanie Hutin, Philippe J. Mas, Petr Man, Eric Forest, Darren J. Hart, Christophe N. Peyrefitte, Wim P. Burmeister, Frédéric Iseni |
| Source: |
Nature Communications, Vol 8, Iss 1, Pp 1-12 (2017) |
| Publisher Information: |
Nature Portfolio, 2017. |
| Publication Year: |
2017 |
| Collection: |
LCC:Science |
| Subject Terms: |
Science |
| More Details: |
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. |
| Document Type: |
article |
| File Description: |
electronic resource |
| Language: |
English |
| ISSN: |
2041-1723 |
| Relation: |
https://doaj.org/toc/2041-1723 |
| DOI: |
10.1038/s41467-017-01542-z |
| Access URL: |
https://doaj.org/article/c56c0fb397134f73a47946a17d780b07 |
| Accession Number: |
edsdoj.56c0fb397134f73a47946a17d780b07 |
| Database: |
Directory of Open Access Journals |
