Annum Munir

Research Article Annum Munir, Stewart Shuman Ann M. Stock, Editor DOI: 10.1128/JB.00292-19 ABSTRACT Runella slithyformis HD-Pnk is the prototype of a family of dual 5′ and 3′ nucleic acid end-healing enzymes that phosphorylate 5′-OH termini and dephosphorylate 2′,3′-cyclic-PO4, 3′-PO4, and 2′-PO4 ends. HD-Pnk is composed of an N-terminal HD phosphohydrolase module and a C-terminal P-loop polynucleotide kinase module.

Research Article Annum Munir, Stewart Shuman DOI: 10.1128/JB.00292-19 ABSTRACT Runella slithyformis HD-Pnk is the prototype of a family of dual 5′ and 3′ nucleic acid end-healing enzymes that phosphorylate 5′-OH termini and dephosphorylate 2′,3′-cyclic-PO4, 3′-PO4, and 2′-PO4 ends. HD-Pnk is composed of an N-terminal HD phosphohydrolase module and a C-terminal P-loop polynucleotide kinase module.

Articles Ushati Das, Li Kai Wang, Paul Smith, Annum Munir, Stewart Shuman DOI: 10.1128/JB.02197-14 ABSTRACT Clostridium thermocellum polynucleotide kinase (CthPnk), the 5′-end-healing module of a bacterial RNA repair system, catalyzes reversible phosphoryl transfer from a nucleoside triphosphate (NTP) donor to a 5′-OH polynucleotide acceptor, either DNA or RNA. Here we report the 1.5-Å crystal structure of CthPnk-D38N in a Michaelis complex with GTP-Mg2+ and a 5′-OH RNA oligonucleotide.