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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(...
| Autores principales: | , , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
Oxford University Press
2014
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3902929/ https://www.ncbi.nlm.nih.gov/pubmed/24150947 http://dx.doi.org/10.1093/nar/gkt936 |