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homotetramer
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4 * 17000, isoforms NDPK In and NDPK IIpn, gel filtration
oligomer
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x * 15000, SDS-PAGE
?
x * 17400, calculated from the deduced amino acid sequence
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x * 25500, calculated from the deduced amino acid sequence
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x * 25700, calculated from the deduced amino acid sequence
?
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x * 16000, deduced from gene sequence
?
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x * 16000, deduced from gene sequence
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x * 18600, SDS-PAGE, x * 18675, mass spectrometry, recombinant protein including 19 amino acid extension
?
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x * 16810, about, MALDI-TOF mass spectrometry
?
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x * 16800, NDK-1, SDS-PAGE
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x * 17800, about, MALDI-TOF mass spectrometry
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x * 17810, about, MALDI-TOF mass spectrometry
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x * 17820, about, MALDI-TOF mass spectrometry
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x * 18590, about, MALDI-TOF mass spectrometry
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x * 17800, about, MALDI-TOF mass spectrometry
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x * 17810, about, MALDI-TOF mass spectrometry
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x * 18600, about, MALDI-TOF mass spectrometry
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x * 18590, about, MALDI-TOF mass spectrometry
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x * 18600, about, MALDI-TOF mass spectrometry
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x * 17870, about, MALDI-TOF mass spectrometry
?
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x * 18590, about, MALDI-TOF mass spectrometry
?
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x * about 15000, SDS-PAGE
?
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x * 14400, SDS-PAGE
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?
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x * 17400, isozyme NDPK2, calculated from amino acid sequence
?
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x * 17900, isozyme NDPK1, calculated from amino acid sequence
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x * 18000, isozyme NDPK3, calculated from amino acid sequence
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x * 25000, precursor protein, x * 18500, and x * 17400, mature enzyme forms
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x * 18500, mature form, SDS-PAGE, x * 25000, precursor form, SDS-PAGE
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x * 16500, isoform NDPK3, calculated from amino acid sequence
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x * 17600, low-molecular weight isoform NDPK2, calculated from amino acid sequence
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x * 18500, high-molecular weight isoform NDPK2, calculated from amino acid sequence
?
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x * 36000, SDS-PAGE under non-reducing conditions
?
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x * 17200, isoform beta, x * 17300, isoform alpha, deduced from gene sequence, major form is alpha
?
x * 19300, SDS-PAGE of recombinant protein including His-tag
?
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x * 41800, SDS-PAGE
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dimer
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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
dimer
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wild-type enzyme
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dimer
2 * 18160, calculated. Wild-type enzyme is a hexamer at 25°C and dissociates to dimer at 35°C in low salt medium
dimer
folded His-tagged enzyme isolated from Escherichia coli forms a hexamer in both 0.2 M and 3.8 M NaCl at 30 °C, while the native enzyme purified from Halobacterium salinarum dissociates to dimer in 0.2 M NaCl
dimer
G114S mutant behaves similarly to wild-type enzyme, dissociating a dimer
dimer
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folded His-tagged enzyme isolated from Escherichia coli forms a hexamer in both 0.2 M and 3.8 M NaCl at 30 °C, while the native enzyme purified from Halobacterium salinarum dissociates to dimer in 0.2 M NaCl
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dimer
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G114S mutant behaves similarly to wild-type enzyme, dissociating a dimer
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dimer
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light scattering and chemical cross-linking experiments
dimer
the sequence of amino acids A-Y-F-F-E-E-S-E of HaNDK is involved in the tetrameric assembly
dimer
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light scattering and chemical cross-linking experiments
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dimer
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tertiary structure homology modelling of wild-type and mutant enzymes using the tetrameric structure of mutagenized HaNDK, PDB ID 3VGU
dimer
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tertiary structure homology modelling of wild-type and mutant enzymes using the tetrameric structure of mutagenized HaNDK, PDB ID 3VGU
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hexamer
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hexamer
x-ray crystallography
hexamer
based on crystallographic symmetry, the enzyme forms a hexamer which is arranged as a trimer of dimers
hexamer
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based on crystallographic symmetry, the enzyme forms a hexamer which is arranged as a trimer of dimers
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hexamer
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6 * 18000, SDS-PAGE
hexamer
exists as a hexamer that is composed of two SDS-stable trimers interacting in a back-to-back association
hexamer
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crystal structure
hexamer
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present as a hexamer under a wide range of salt concentrations (0.2-4 M NaCl)
hexamer
present as a hexamer under a wide range of salt concentrations (0.2-4 M NaCl)
hexamer
2 * 18160, calculated. Wild-type enzyme is a hexamer at 25°C and dissociates to dimer at 35°C in low salt medium. Mutant G114R maintains hexameric structure at both 25 and 35°C
hexamer
folded His-tagged enzyme isolated from Escherichia coli forms a hexamer in both 0.2 M and 3.8 M NaCl at 30 °C, while the native enzyme purified from Halobacterium salinarum dissociates to dimer in 0.2 M NaCl
hexamer
G114K mutant has a hexameric structure under low salt concentration of non-denaturing PAGE condition
hexamer
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folded His-tagged enzyme isolated from Escherichia coli forms a hexamer in both 0.2 M and 3.8 M NaCl at 30 °C, while the native enzyme purified from Halobacterium salinarum dissociates to dimer in 0.2 M NaCl
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hexamer
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G114K mutant has a hexameric structure under low salt concentration of non-denaturing PAGE condition
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hexamer
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erythrocyte: different heterohexamers of isoforms A,B, main form is 3 * A + 3 * B, placenta: pure isoform B and heteromeric 1:1 mixture of isoforms A,B, SDS-PAGE
hexamer
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x * 19000 + x * 20500, SDS-PAGE
hexamer
x-ray crystallography
hexamer
6 * 17000-21000, the cytosolic isozymes form heterohexameric complexes
hexamer
MgATP promotes correct folding and association, but MgATP does not shift the equilibrium between the folding intermediate and the native monomer in the presence of 2-3 M urea. The molten globule folding intermediate can bind ATP and be autophosphorylated
hexamer
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wild-type enzyme, but not catalytically inactive H118C mutant isozyme NDPKB, undergoes dynamic self-assembly into ordered 20-25 nm diameter filaments in vitro. Self-assembly is nucleoside triphosphate dependent, GTP being most effective at promoting polymer formation, polymerization also depends on formation of a phosphoryl-His intermediate of the enzyme, mechanism, overview
hexamer
x-ray crystallography
hexamer
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x-ray crystallography
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hexamer
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6 * 23000, SDS-PAGE
hexamer
6 * 17000, crystal structure analysis
hexamer
crystal structure analysis
hexamer
monomers are arranged as trimers of dimers, crystal structure analysis
hexamer
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6 * 17000-21000, the cytosolic isozymes form heterohexameric complexes
hexamer
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6 * 17000, about
hexamer
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6 * 17860, high speed sedimentation equilibrium in 4 M guanidinium chloride
hexamer
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6 * 17300, SDS-PAGE
hexamer
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6 * 16000, isozyme I, SDS-PAGE
hexamer
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6 * 18000, SDS-PAGE, isozyme II
hexamer
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6 * 17000, SDS-PAGE
homodimer
2 * 15159, calculated from amino acid sequence
homodimer
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2 * 15159, calculated from amino acid sequence
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homodimer
2 * 15137, calculated from amino acid sequence
homohexamer
assembled as a trimer of basic dimeric units
homohexamer
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assembled as a trimer of basic dimeric units
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homohexamer
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6 * 18675, dynamic light scattering
monomer
enzyme mutant C139S
monomer
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enzyme mutant C139S
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monomer
enzyme mutant C139S
tetramer
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tetramer
the enzyme exists predominantly in form of tetramer in solution. The tetrameric form with dimer-dimer interaction is crucial for its function. The dimeric enzyme form loses the kinase activity and is lethal for Aspergillus fumigatus
tetramer
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the enzyme exists predominantly in form of tetramer in solution. The tetrameric form with dimer-dimer interaction is crucial for its function. The dimeric enzyme form loses the kinase activity and is lethal for Aspergillus fumigatus
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tetramer
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the enzyme shows a tetrameric quaternary structure, the relative orientation of interacting dimers facing either the convex or the concave side of their central sheet, overview
tetramer
mutant enzyme E134A
tetramer
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4 * 17000, about, SDS-PAGE
tetramer
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4 * 17000, about, SDS-PAGE
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tetramer
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4 * 16000, crystal structure
tetramer
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4 * 15000, about
tetramer
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the sequence of amino acids A-Y-F-F-AA-T-E of PaNDK is involved in the tetrameric assembly
tetramer
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4 * 18000, SDS-PAGE under reducing conditions
tetramer
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4 * 17000-18000, SDS-PAGE
tetramer
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4 * 15000, SDS-PAGE
tetramer
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4 * 15000, calculated from the deduced amino acid sequence, SDS-PAGE, native mass by gel filtration
tetramer
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4 * 15000, calculated from the deduced amino acid sequence, SDS-PAGE, native mass by gel filtration
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trimer
gel filtration and analytical ultracentrifugation
additional information
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overview on enzyme structure
additional information
three-dimensional structure structure modeling
additional information
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three-dimensional structure structure modeling
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additional information
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overview on enzyme structure
additional information
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overview on enzyme structure
additional information
the asymmetric enzyme unit is made of three molecules, each of which consists of a four-stranded anti-parallel beta-sheets and seven alpha-helices, the simulated nucleotide-binding active site is conserved, structure analysis and modelling, overview
additional information
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the asymmetric enzyme unit is made of three molecules, each of which consists of a four-stranded anti-parallel beta-sheets and seven alpha-helices, the simulated nucleotide-binding active site is conserved, structure analysis and modelling, overview
additional information
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recombinant nucleoside-diphosphate kinase interacts with uracil DNA-glycosylase Ung in specific and direct manner. The interaction significantly augments Ung catalytic activity
additional information
mutant G114R runs faster on SDS-PAGE than wild-type
additional information
a basic amino acid at residue 114 is responsible for the stabilization of subunit assembly
additional information
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a basic amino acid at residue 114 is responsible for the stabilization of subunit assembly
additional information
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a basic amino acid at residue 114 is responsible for the stabilization of subunit assembly
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additional information
three-dimensional structure structure modeling
additional information
structure modeling of wild-type and mutant enzyme, overview
additional information
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overview on enzyme structure
additional information
three-dimensional structure of NDPK B complexed with a heterotrimeric G protein, NDPK B/Gbetagamma complex formation, structure, and mode of action, overview
additional information
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peptide mapping by MALDI-TOF mass spectrometry, detailed overview
additional information
peptide mapping by MALDI-TOF mass spectrometry, detailed overview
additional information
peptide mapping by MALDI-TOF mass spectrometry, detailed overview
additional information
peptide mapping by MALDI-TOF mass spectrometry, detailed overview
additional information
peptide mapping by MALDI-TOF mass spectrometry, detailed overview
additional information
peptide mapping by MALDI-TOF mass spectrometry, detailed overview
additional information
peptide mapping by MALDI-TOF mass spectrometry, detailed overview
additional information
peptide mapping by MALDI-TOF mass spectrometry, detailed overview
additional information
peptide mapping by MALDI-TOF mass spectrometry, detailed overview
additional information
peptide mapping by MALDI-TOF mass spectrometry, detailed overview
additional information
peptide mapping by MALDI-TOF mass spectrometry, detailed overview
additional information
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peptide mapping by MALDI-TOF mass spectrometry, detailed overview
additional information
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the intersubunit salt bridge Arg80-Asp93 contributes to the thermal stability of the hexamer
additional information
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binds to cellular proteins of 70, 65, 60, or 50 kDa which modulate specificity
additional information
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overview on enzyme structure
additional information
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stable in NaCl between 0 and 3.5 M
additional information
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interaction of enzyme with catalase isoform Cat-1
additional information
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the enzyme has a molecular weight of 60-120 kDa
additional information
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structure modeling of wild-type and mutant enzyme, overview
additional information
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overview on enzyme structure
additional information
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enzyme interacts with G protein betagamma complex. Receptor-independent activation of G proteins via enzyme isoform B/G protein betagamma complexes requires the intermediate phosphorylation of G protein subunit beta at H266
additional information
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three-dimensional structure of NDPK B complexed with a heterotrimeric G protein, NDPK B/Gbetagamma complex formation, structure, and mode of action, overview
additional information
the cytosolic enzyme, fused to GFP, generates large granules that depend on its quaternary, oligomeric structure, overview
additional information
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the cytosolic enzyme, fused to GFP, generates large granules that depend on its quaternary, oligomeric structure, overview
additional information
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the cytosolic enzyme, fused to GFP, generates large granules that depend on its quaternary, oligomeric structure, overview
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additional information
NDPK1 is a short enzyme isoform, whereas NDPK2 is a long one containing a DM10 motif