Sensitivity of the C-Terminal Nuclease Domain of Kaposi's Sarcoma-Associated Herpesvirus ORF29 to Two Classes of Active-Site Ligands.

ABSTRACT: Kaposi's sarcoma-associated herpesvirus (KSHV), the etiological agent of Kaposi's sarcoma, belongs to the Herpesviridae family, whose members employ a multicomponent terminase to resolve nonparametric viral DNA into genome-length units prior to their packaging. Homology modeling of the ORF29 C-terminal nuclease domain (pORF29C) and bacteriophage Sf6 gp2 have suggested an active site clustered with four acidic residues, D⁴⁷⁶, E⁵⁵⁰, D⁶⁶¹, and D⁶⁶², that collectively sequester the catalytic divalent metal (Mn²⁺) and also provided important insight into a potential inhibitor binding mode. Using this model, we have expressed, purified, and characterized the wild-type pORF29C and variants with substitutions at the proposed active-site

SUBMITTER: Miller JT 

PROVIDER: S-EPMC6153795 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature