Literature summary for 2.7.4.6 extracted from
Hu, Y.; Feng, F.; Liu, Y.
Structural and functional characterization of Acinetobacter baumannii nucleoside diphosphate kinase (2015), Prog. Biochem. Biophys., 42, 260-267.
No PubMed abstract available
Application
Application |
Comment |
Organism |
drug development |
the enzyme is a potential target to develop therapeutic approaches to overcome multiresistance of the bacterium against antibiotics |
Acinetobacter baumannii |
Cloned(Commentary)
Cloned (Comment) |
Organism |
gene ndk, recombinant expression of tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) |
Acinetobacter baumannii |
Crystallization (Commentary)
Crystallization (Comment) |
Organism |
purified recombinant tagged wild-type and mutant enzymes, hanging-drop vapor diffusion method, mixing of 0.001 ml of spontanously degraded 200 mg/ml protein in 50 mmol/L Tris, pH 8.0, 150 mmol/l NaCl, and 5 mmol/l MgCl2, with 0.001 ml of reservoir solution containing 0.1 mol/l potassium sodium tartrate tetrahydrate, and 18% w/v PEG 3350 for the wild-type enzyme and 1 mol/l sodium malonate, pH 7.0, 0.1 mol/l HEPES, pH 7.0, and 0.5% v/v Jeffamine ED-2001, pH 7.0 for the truncated mutant enzymes, X-ray diffraction structure determination and analysis, molecular replacement method using Burkholderia thailandensis NDK, PDB ID 4DUT, as starting model |
Acinetobacter baumannii |
Protein Variants
Protein Variants |
Comment |
Organism |
E28A |
site-directed mutagenesis the mutation interrupts the secondary structure of the protein leading to declined enzymatic activity compared to wild-type |
Acinetobacter baumannii |
additional information |
construction of a C-terminally truncated mutant, truncation of the C-terminal arginine-threonine-arginine (RTR) residues leads to the instability of the tertiary structure resulting in reduced kinase activity compared to wild-type, mutant crystal structure analysis |
Acinetobacter baumannii |
Metals/Ions
Metals/Ions |
Comment |
Organism |
Structure |
Mg2+ |
required |
Acinetobacter baumannii |
|
Organism
Organism |
UniProt |
Comment |
Textmining |
Acinetobacter baumannii |
- |
- |
- |
Purification (Commentary)
Purification (Comment) |
Organism |
recombinant tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by affinity chromatography and gel filtration |
Acinetobacter baumannii |
Substrates and Products (Substrate)
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
GTP + ADP |
- |
Acinetobacter baumannii |
GDP + ATP |
- |
? |
|
additional information |
the enzyme catalyzes transfer of the gamma-phosphate from a nucleoside triphosphate (NTP) to a nucleoside diphosphate (NDP) |
Acinetobacter baumannii |
? |
- |
? |
|
Subunits
Subunits |
Comment |
Organism |
dimer |
Lys33 is a key residue for maintaining dimer interaction when RTR residues are truncated but is not sufficient to keep efficient enzymatic reaction of the C-terminally truncated mutant enzyme |
Acinetobacter baumannii |
Synonyms
Synonyms |
Comment |
Organism |
NDK |
- |
Acinetobacter baumannii |
nucleoside diphosphate kinase |
- |
Acinetobacter baumannii |
Temperature Optimum [°C]
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
22 |
- |
assay at room temperature |
Acinetobacter baumannii |
pH Optimum
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
8 |
- |
assay at |
Acinetobacter baumannii |
General Information
General Information |
Comment |
Organism |
additional information |
Acinetobacter baumannii NDK structure comparison with the structure of the Myxococcus xanthus enzyme NDK. Acinetobacter baumannii NDK might share a similar catalytic mechanism with Myxococcus xanthus NDK |
Acinetobacter baumannii |