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The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding
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SYSNO ASEP 0482204 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding Author(s) Tarbouriech, N. (FR)
Ducournau, C. (FR)
Hutin, S. (FR)
Mas, P.J. (FR)
Man, Petr (MBU-M) RID, ORCID
Forest, E. (FR)
Hart, D.J. (FR)
Peyrefitte, Ch.N. (FR)
Burmeister, W.P. (FR)
Iseni, F. (FR)Article number 1455 Source Title Nature Communications. - : Nature Publishing Group
Roč. 8, NOV 13 (2017), s. 1-12Number of pages 12 s. Language eng - English Country GB - United Kingdom Keywords PROTEIN SECONDARY STRUCTURE ; CRYSTAL-STRUCTURE ; GENETIC-CHARACTERIZATION Subject RIV CE - Biochemistry OECD category Biochemistry and molecular biology R&D Projects LQ1604 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Institutional support MBU-M - RVO:61388971 UT WOS 000414915900017 EID SCOPUS 85033776744 DOI 10.1038/s41467-017-01542-z Annotation Vaccinia virus (VACV), the prototype member of the Poxviridae, replicates in the cytoplasm of an infected cell. The catalytic subunit of the DNA polymerase E9 binds the heterodimeric processivity factor A20/D4 to form the functional polymerase holoenzyme. Here we present the crystal structure of full-length E9 at 2.7 angstrom resolution that permits identification of important poxvirus-specific structural insertions. One insertion in the palm domain interacts with C-terminal residues of A20 and thus serves as the processivity factor-binding site. This is in strong contrast to all other family B polymerases that bind their co-factors at the C terminus of the thumb domain. The VACV E9 structure also permits rationalization of polymerase inhibitor resistance mutations when compared with the closely related eukaryotic polymerase delta-DNA complex. Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2018
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