Crystal structure of the human Polϵ B-subunit in complex with the C-terminal domain of the catalytic subunit.

ABSTRACT: The eukaryotic B-family DNA polymerases include four members: Polα, Polδ, Polϵ, and Polζ, which share common architectural features, such as the exonuclease/polymerase and C-terminal domains (CTDs) of catalytic subunits bound to indispensable B-subunits, which serve as scaffolds that mediate interactions with other components of the replication machinery. Crystal structures for the B-subunits of Polα and Polδ/Polζ have been reported: the former within the primosome and separately with CTD and the latter with the N-terminal domain of the C-subunit. Here we present the crystal structure of the human Polϵ B-subunit (p59) in complex with CTD of the catalytic subunit (p261_C). The structure revealed a well defined electron density for p261_C and the phosphodiesterase and oli

SUBMITTER: Baranovskiy AG 

PROVIDER: S-EPMC5612105 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature