4HX9
Designed Phosphodeoxyribosyltransferase
Summary for 4HX9
| Entry DOI | 10.2210/pdb4hx9/pdb |
| Descriptor | Nucleoside deoxyribosyltransferase, SULFATE ION, TETRAETHYLENE GLYCOL, ... (4 entities in total) |
| Functional Keywords | non natural and design enzyme, rossmann fold, phosphodeoxyribosyltransferase, transferase |
| Biological source | Lactobacillus leichmannii |
| Total number of polymer chains | 8 |
| Total formula weight | 146704.65 |
| Authors | Kaminski, P.A.,Labesse, G. (deposition date: 2012-11-09, release date: 2013-01-16, Last modification date: 2023-09-20) |
| Primary citation | Kaminski, P.A.,Labesse, G. Phosphodeoxyribosyltransferases, designed enzymes for deoxyribonucleotides synthesis. J.Biol.Chem., 288:6534-6541, 2013 Cited by PubMed Abstract: A large number of nucleoside analogues and 2'-deoxynucleoside triphosphates (dNTP) have been synthesized to interfere with DNA metabolism. However, in vivo the concentration and phosphorylation of these analogues are key limiting factors. In this context, we designed enzymes to switch nucleobases attached to a deoxyribose monophosphate. Active chimeras were made from two distantly related enzymes: a nucleoside deoxyribosyltransferase from lactobacilli and a 5'-monophosphate-2'-deoxyribonucleoside hydrolase from rat. Then their unprecedented activity was further extended to deoxyribose triphosphate, and in vitro biosyntheses could be successfully performed with several base analogues. These new enzymes provide new tools to synthesize dNTP analogues and to deliver them into cells. PubMed: 23325804DOI: 10.1074/jbc.M112.446492 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.68 Å) |
Structure validation
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