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Structures of Bacterial Polynucleotide Kinase in a Michaelis Complex with Nucleoside Triphosphate (NTP)-Mg2+ and 5′-OH RNA and a Mixed Substrate-Product Complex with NTP-Mg2+ and a 5′-Phosphorylated Oligonucleotide

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By Paul Smith Verified, Annum Munir, Stewart Shuman, Ushati Das
| asm.org
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.
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