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2.7.1.145: deoxynucleoside kinase

This is an abbreviated version!
For detailed information about deoxynucleoside kinase, go to the full flat file.

Word Map on EC 2.7.1.145

Reaction

ATP
+
a 2'-deoxyribonucleoside
=
ADP
 +
a 2'-deoxyribonucleoside 5'-phosphate

Synonyms

AGCK, AgdNK, BmdNK, D. melanogaster deoxynucleoside kinase, deoxyribonucleoside kinase, deoxyribonucleoside kinase , deoxyribonucleoside phosphotransferase, Dm-dNK, DmdNK, dNK, kinase (phosphorylating), deoxynucleoside, More, ms-dNK, multi-substrate deoxyribonucleoside kinase, multifunctional deoxynucleoside kinase, multispecific deoxynucleoside kinase, multisubstrate deoxyribonucleoside kinase, nucleoside triphosphate: deoxyribonucleoside 5'-phosphotransferase, pyrimidine deoxyribonucleoside kinase, white stripe leaf8, WSL8, Xen-PyK

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.1 Phosphotransferases with an alcohol group as acceptor
                2.7.1.145 deoxynucleoside kinase

Crystallization

Crystallization on EC 2.7.1.145 - deoxynucleoside kinase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure determination, PDB IDs 1OE0, 1OT3, 1J90, 1ZM7, 1ZMX, 2JCS, 2VP0, 2VP2, 2VP4, 2VP, 2VP6, 2VP9, 2VPP, 2VQ, and 2JJ8
crystals of a C-terminally truncated (D20) recombinant Dm-dNK mutant E52D are grown using the vapour diffusion method by hanging drop geometry. The E52D mutant is crystallized with its feedback inhibitor dTTP. The backbone conformation remains unchanged, and coordination between D52 and the dTTP–Mg complex is observed
-
in complex with floxuridine, brivudine, zidovudine, zalcitabine, or dCTP or dGTP with resolution of 2.2-2.9 A. dCTP and dGTP bind with the base in the substrate site, similarly to feedback inhibitor dTTP. Contrary to nucleoside analogs, dGTP adopts a syn conformation
purified recombinant enzyme in complex with dT and dTPP, hanging drop vapour diffusion method, enzyme solution containing 5-10 mg/ml protein, 5 mM dT or dTTP, is mixed in equal volumes with cyrstallization solution containing 0.1 M MES, pH 6.5, 0.2 M ammonium sulfate, 18-22% w/v PEG 5000 monomethylether, and 5-10% w/v PEG 400, 3-5 days, 14°C, X-ray diffraction structure determination and analysis at 2.4-2.5 A resolution
purified recombinant enzyme, hanging drop vapour diffusion method, enzyme solution containing 10 mg/ml protein and 10 mM deoxycytidine, mixed with an equal volume of cyrstallization solution containing 0.1 M MES, pH 6.5, 0.2 M ammonium sulfate, 20% w/v PEG 5000, and 8-10% v/v PEG 400, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement method
purified recombinant mutant N64D in complex with dT or dTTP, counter diffusion and vapour diffusion methods, 20 mg/ml enzyme with 10 mM dT, is mixed with cyrstallization solution containing 0.15 M MES, pH 6.5, 0.3 M lithium sulfate, and 27,5% w/v PEG 2000 monomethylether, or 10 mg/ml enzyme with 5 mM dTTP is mixed with 0.1 M MES, pH 6.5, 0.16 M lithium sulfate, and 25% v/v PEG 2000 monomethylether, 2 weeks, 15°C, X-ray diffraction structure determination and analysis at 3.1 A and 2.2 A resolution, respectively
-
truncated dNK lacking the last 20 amino acid residues in complex with gemcitabine, hanging drop vapor diffusion method, using 0.1 M MES pH 6.5, 0.2 M lithium sulfate and 26% (w/v) mPEG2000