{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Miller JT"],"funding":["HHS | National Institutes of Health","CCR NIH HHS","HHS | NIH | National Institute of General Medical Sciences","HHS | NIH | National Cancer Institute","NCI NIH HHS","NIGMS NIH HHS"],"pagination":["e00233-18"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6153795"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["62(10)"],"pubmed_abstract":["Kaposi's sarcoma-associated herpesvirus (KSHV), the etiological agent of Kaposi's sarcoma, belongs to the <i>Herpesviridae</i> 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, D<sup>476</sup>, E<sup>550</sup>, D<sup>661</sup>, and D<sup>662</sup>, that collectively sequester the catalytic divalent metal (Mn<sup>2+</sup>) 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"],"journal":["Antimicrobial agents and chemotherapy"],"pubmed_title":["Sensitivity of the C-Terminal Nuclease Domain of Kaposi's Sarcoma-Associated Herpesvirus ORF29 to Two Classes of Active-Site Ligands."],"pmcid":["PMC6153795"],"funding_grant_id":["R01 GM090010","SC1 GM111158","HHSN261200800001E","R01GM090010","HHSN261200800001C","SC1GM111158"],"pubmed_authors":["Miller JT","Aron KE","Hirsch DR","Kouhestani K","Cornejo Castro EM","Marshall VA","Tang L","Le Grice SFJ","Murelli RP","Varnado B","Xia A","Beutler JA","Whitby D","Zhao H","Masaoka T","Lynn AY"],"additional_accession":[]},"is_claimable":false,"name":"Sensitivity of the C-Terminal Nuclease Domain of Kaposi's Sarcoma-Associated Herpesvirus ORF29 to Two Classes of Active-Site Ligands.","description":"Kaposi's sarcoma-associated herpesvirus (KSHV), the etiological agent of Kaposi's sarcoma, belongs to the <i>Herpesviridae</i> 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, D<sup>476</sup>, E<sup>550</sup>, D<sup>661</sup>, and D<sup>662</sup>, that collectively sequester the catalytic divalent metal (Mn<sup>2+</sup>) 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","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Oct","modification":"2026-06-14T04:19:55.78Z","creation":"2026-06-14T03:09:08.253Z"},"accession":"S-EPMC6153795","cross_references":{"pubmed":["30061278"],"doi":["10.1128/aac.00233-18","10.1128/AAC.00233-18"]}}