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Structures of bacterial polynucleotide kinase in a Michaelis complex with GTP•Mg(2+) and 5′-OH oligonucleotide and a product complex with GDP•Mg(2+) and 5′-PO(4) oligonucleotide reveal a mechanism of general acid-base catalysis and the determinants of phosphoacceptor recognition

Clostridium thermocellum polynucleotide kinase (CthPnk), the 5′ end-healing module of a bacterial RNA repair system, catalyzes reversible phosphoryl transfer from an NTP donor to a 5′-OH polynucleotide acceptor. Here we report the crystal structures of CthPnk-D38N in a Michaelis complex with GTP•Mg(...

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Hlavní autoři: Das, Ushati, Wang, Li Kai, Smith, Paul, Jacewicz, Agata, Shuman, Stewart
Médium: Artigo
Jazyk:Inglês
Vydáno: Oxford University Press 2014
Témata:
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC3902929/
https://ncbi.nlm.nih.gov/pubmed/24150947
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/nar/gkt936
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