4hx9

Designed Phosphodeoxyribosyltransferase

spinqualitylabelsall models 4hx9, resolution 2.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4hx9 is a 8 chain structure with sequence from Lactobacillus leichmannii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.68Å Ligands: PG4, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NTD_LACLE Catalyzes the cleavage of the glycosidic bond of 2'-deoxyribonucleosides and the transfer of the deoxyribosyl moiety to an acceptor purine or pyrimidine base. Publication Abstract from PubMed A large number of nucleoside analogs and 2'- deoxynucleoside triphosphates (dNTPs) have been synthesized in order 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 (NDT) from lactobacilli and a 5'-monophosphate-2'-deoxyribonucleoside hydrolase (Rcl) 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 dNTPs analogs and to deliver them into cells. Phosphodeoxyribosyltransferases: designed enzymes for deoxyribonucleotide synthesis.,Kaminski PA, Labesse G J Biol Chem. 2013 Jan 16. PMID:23325804 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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