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2.7.1.32: choline kinase

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

Word Map on EC 2.7.1.32

Reaction

ATP
+
choline
=
ADP
 +
phosphocholine

Synonyms

ATP/choline phosphotransferase, ATP:choline phosphotransferase, CEK1, CEK2, CEK3, chbA, CHETK-alpha, CHK, chk-alpha, Chka, CHKA2, ChKalpha, ChoK, ChoK alpha, ChoKalpha, CHOKalpha1, ChoKalpha2, ChoKbeta1, choline kinase, choline kinase alpa, choline kinase alpha, choline kinase alpha1, choline kinase alpha2, choline kinase beta, choline kinase beta1, choline kinase isoform alpha2, choline kinase-alpha, choline phosphokinase, choline-ethanolamine kinase, choline/ethanolamine kinase, choline/ethanolamine kinase 1, choline/ethanolamine kinase 2, choline/ethanolamine kinase 3, CK, CK-alpha, CK-alpha1, CK-alpha1/beta, CK-alpha2, CK-beta, CK1, CK2, CK3, CKA-2, CKalpha, CKalpha1, CKalpha2, ckb, CKbeta, CKbeta1, CKI1, CKI1-encoded choline kinase, CKII, ER-localized Cho kinase, EtnK, hChoK, kinase, choline (phosphorylating), LicA, LinfC/EK35, More, PfChoK, PfCK, protein LicA, putative choline kinase, sChoK, TbC/EK2

ECTree

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

Crystallization

Crystallization on EC 2.7.1.32 - choline kinase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with inhibitor V-11-023907, hanging drop vapor diffusion method, using 0.1 M Bis-Tris (pH 6.5), 25% (w/v) polyethylene glycol 3350, and 0.1 M MgCl2
in complex with inhibitors, hanging drop vapor diffusion method, using 10-30% (w/v) polyethylene glycol 5000 monomethyl ether and 0.2 M magnesium phormate
isoform ChoKalpha1 in complex with hemicholinium-3 and ADP, sitting drop vapor diffusion method, using 0.1 M HEPES (pH 7.5), 25% (w/v) polyethylene glycol 3350, and 0.2 M lithium sulfate
isoform ChoKbeta in complex with hemicholinium-3 and ADP, sitting drop vapor diffusion method, using 0.1 M sodium cacodylate (pH 6.5), 30% polyethylene glycol 4000, and 0.2 M ammonium sulfate
purified choline kinase catalytic domain of the protein, residues 80-457, and of SH3-ChoKalpha1(60-69) fusion protein, from 0.2 M zinc acetate, 0.1 M imidazole pH 8.0, and 20% w/v PEG 3000, drops of 0.002 ml protein at 10 mg/ml are set at a 1:1 ratio with reservoir solution, 2-3 weeks, X-ray diffraction structure determination and analysis at 1.5 A resolution, structure modeling using the structure of c-Src-SH3 with the NS5A peptide, PDB ID 4QT7, as a model
purified recombinant isozyme ChoKalpha truncated mutant DELTA79 in apoform and in complex with inhibitor TCD-717, sitting drop vapor diffusion method, mixing of 0.002 ml of 10 mg/ml protein solution with 0.002 ml of reservoir solution containing 0.1 M MES, pH 6.5, and 20% PEG 3350, 2-3 days, 20°C, crystals are soaked with TCD-717 by mixing a 50 mM solution of 100% DMSO-resuspended compound in a 1:4 ratio with the reservoir buffer, X-ray diffraction structure determination and analysis at 2.35 A resolution
purified recombinant tagged enzyme in apoform and in complex with inhibitor 1-[4-[(4-methyl-1,4-diazepan-1-yl)methyl]phenyl]methanamine, mixing of 30 mg/ml protein solution with 0.1 M sodium formate, 8-12% PEG 3350 at 18°C, complex structures are obtained by soaking the inhibitors into the ChoKalpha1 crystals at a final concentration of 2-5 mM for 45-60 min before freezing in liquid nitrogen, X-ray diffraction structrue determination and analysis, modelling
sitting drop vapor diffusion method, using 20% (w/v) polyethylene glycol 3350 and 0.25 M potassium isothiocyanate
sitting drop vapour diffusion using 25 mM Tris/HCl (pH 7.5), 25 mM KCl, 0.5 mM dithiothreitol, 0.0005 ml of 0.1 M MgCl2 in 12-20% PEG 3350 with 0.2 M NaF
using 0.1 M sodium formate, 8-12% (w/v) PEG 3350 at 18°C
purified recombinat His6-tagged choline kinase in apoform and in ADP-bound form, hanging drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein solution with 0.001 ml of reservoir solution, and equilibration against 0.5 ml reservoir solution, containing 16% v/v PEG 8000, 0.2 M NaCl, 0.1 M HEPES, pH 7.5, 2 mM Tris(2-carboxyethyl)phosphine (TCEP), and 4 mM MgCl2 for the apoform crystals, and the same composition with 2 mM ADP for the complex crystals, at room temperature, X-ray diffraction structrue determination and analysis at 2.0-2.2 A resolution, molecular replacement and model building using the PDB ID 3FI8 structure as starting model
native and selenomethionine-labelled enzyme, hanging drop vapor diffusion method, using 0.1M HEPES, pH 7.5, 1.2 M sodium citrate and 4% (v/v) glycerol