Počet záznamů: 1  

The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding

  1. 1.
    0482204 - MBU-M 2018 RIV GB eng J - Článek v odborném periodiku
    Tarbouriech, N. - Ducournau, C. - Hutin, S. - Mas, P.J. - Man, Petr - Forest, E. - Hart, D.J. - Peyrefitte, Ch.N. - Burmeister, W.P. - Iseni, F.
    The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding.
    Nature Communications. Roč. 8, NOV 13 (2017), s. 1-12, č. článku 1455. ISSN 2041-1723
    Grant CEP: GA MŠk(CZ) LQ1604
    Institucionální podpora: RVO:61388971
    Klíčová slova: PROTEIN SECONDARY STRUCTURE * CRYSTAL-STRUCTURE * GENETIC-CHARACTERIZATION
    Kód oboru RIV: CE - Biochemie
    Obor OECD: Biochemistry and molecular biology
    Impakt faktor: 12.353, rok: 2017

    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.
    Trvalý link: http://hdl.handle.net/11104/0277586