BRENDA - Enzyme Database
show all sequences of 2.7.1.B20

Structure of Methanocaldococcus jannaschii nucleoside kinase: an archaeal member of the ribokinase family

Arnfors, L.; Hansen, T.; Schönheit, P.; Ladenstein, R.; Meining, W.; Acta Crystallogr. Sect. D 62, 1085-1097 (2006)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization (Commentary)
Organism
sitting- and hanging-drop vapour diffusion methods, three-dimensional structures of the unliganded enzyme and a complex of the enzyme, an ATP analogue and adenosine are determined to 1.7 and 1.9 A resolution, respectively. In the crystal structure of the MjNK complex, subunit A adopts a closed conformation and subunit B an open conformation. In subunit A all substrates and Mg2+ are observed, whereas in subunit B only the ATP analogue can be clearly identified in the electron density
Methanocaldococcus jannaschii
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
there are two magnesium-binding sites per subunit: one Mg2+ (MO6) is coordinated octahedrally by six water molecules and is located between adenosine and AMPPNP in the active site and one Mg2+ (MO5) is coordinated by five water molecules and is positioned in the interface between the dimers in the crystal
Methanocaldococcus jannaschii
Organism
Organism
UniProt
Commentary
Textmining
Methanocaldococcus jannaschii
Q57849
-
-
Methanocaldococcus jannaschii DSM 2661
Q57849
-
-
Synonyms
Synonyms
Commentary
Organism
MJ0406
locus name
Methanocaldococcus jannaschii
MjNK
-
Methanocaldococcus jannaschii
nucleoside kinase
-
Methanocaldococcus jannaschii
Crystallization (Commentary) (protein specific)
Crystallization
Organism
sitting- and hanging-drop vapour diffusion methods, three-dimensional structures of the unliganded enzyme and a complex of the enzyme, an ATP analogue and adenosine are determined to 1.7 and 1.9 A resolution, respectively. In the crystal structure of the MjNK complex, subunit A adopts a closed conformation and subunit B an open conformation. In subunit A all substrates and Mg2+ are observed, whereas in subunit B only the ATP analogue can be clearly identified in the electron density
Methanocaldococcus jannaschii
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
there are two magnesium-binding sites per subunit: one Mg2+ (MO6) is coordinated octahedrally by six water molecules and is located between adenosine and AMPPNP in the active site and one Mg2+ (MO5) is coordinated by five water molecules and is positioned in the interface between the dimers in the crystal
Methanocaldococcus jannaschii
Other publictions for EC 2.7.1.B20
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
728780
Elkin
A broad specificity nucleoside ...
Thermoplasma acidophilum
Proteins
81
568-582
2013
-
-
1
1
-
-
-
6
1
3
2
-
-
4
-
-
1
-
-
-
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7
1
1
1
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6
2
1
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1
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1
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6
1
3
2
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1
-
-
-
-
7
1
1
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6
2
1
-
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-
-
-
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6
6
697882
Ota
A novel nucleoside kinase from ...
Burkholderia thailandensis, Burkholderia thailandensis DSM 13276
FEBS J.
275
5865-5872
2008
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-
1
-
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2
8
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3
2
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7
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1
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18
1
2
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3
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1
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1
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2
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8
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3
2
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1
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18
1
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3
-
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1
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8
8
726575
Arnfors
Structure of Methanocaldococcu ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661
Acta Crystallogr. Sect. D
62
1085-1097
2006
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1
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1
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8
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3
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1
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727430
Hansen
The phosphofructokinase-B (MJ0 ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661
Extremophiles
11
105-114
2006
-
-
1
-
-
-
-
4
-
4
2
2
-
9
-
-
1
-
-
-
-
-
16
1
3
1
-
1
-
1
1
-
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-
1
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-
-
-
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4
-
4
2
2
-
-
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1
-
-
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16
1
1
-
1
-
1
1
-
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-
1
1
-
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-
726601
Arnfors
Expression, purification, crys ...
Methanocaldococcus jannaschii
Acta Crystallogr. Sect. F
61
591-594
2005
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1
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2
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1
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1
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1
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1
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