BRENDA - Enzyme Database show
show all sequences of 4.2.1.80

Assembly of a 20-nm protein cage by Escherichia coli 2-hydroxypentadienoic acid hydratase

Montgomery, M.G.; Coker, A.R.; Taylor, I.A.; Wood, S.P.; J. Mol. Biol. 396, 1379-1391 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
ligated into a modified pET22b expression vector encoding a His6 tag and expressed in Escherichia coli BL21(DE3) cells
Escherichia coli K-12
Crystallization (Commentary)
Crystallization
Organism
MhpD with and without Mg2+, by hanging-drop vapour-diffusion method, to 2.8 A resolution. Space group of the crystals is H3 with unit cell parameters a = 207.35 A, b = 207.35 A, c = 545.47 A, alpha = 90°, beta = 90°, and gamma = 120°. Assembles to form a 20-nm-diameter particle comprising 60 protein subunits, arranged with 532 symmetry when crystallised at low pH in the presence of phosphate or sulphate ions. Particles form rapidly and are stable in solution during gel filtration at low pH. They are probably formed through trimers of pentamers, which are stabilised by the interaction of two phosphate ions with residues of the N-terminal domains of subunits at the 3fold axis. Once the particles are formed at high concentrations of phosphate (or sulphate), they remain stable in solution at 20fold lower concentrations of the anion. Guest molecules can be trapped within the hollow protein shell during assembly. The C-termini of the subunits are freely accessible on the surface of the protein cage
Escherichia coli K-12
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
active site of MhpD consists of three acidic residues (Glu105, Glu107, and Glu138), which may be involved in coordinating the divalent cation essential for activity
Escherichia coli K-12
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
30000
-
5 * 35000, fusion protein, SDS-PAGE. 5 * 30000, purified protein, SDS-PAGE
Escherichia coli K-12
35000
-
5 * 35000, fusion protein, SDS-PAGE. 5 * 30000, purified protein, SDS-PAGE
Escherichia coli K-12
151000
-
gel filtration-multiangle laser light scattering
Escherichia coli K-12
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli K-12
P77608
-
-
Purification (Commentary)
Commentary
Organism
by centrifugation and gel filtration
Escherichia coli K-12
Subunits
Subunits
Commentary
Organism
pentamer
5 * 35000, fusion protein, SDS-PAGE. 5 * 30000, purified protein, SDS-PAGE
Escherichia coli K-12
Cloned(Commentary) (protein specific)
Commentary
Organism
ligated into a modified pET22b expression vector encoding a His6 tag and expressed in Escherichia coli BL21(DE3) cells
Escherichia coli K-12
Crystallization (Commentary) (protein specific)
Crystallization
Organism
MhpD with and without Mg2+, by hanging-drop vapour-diffusion method, to 2.8 A resolution. Space group of the crystals is H3 with unit cell parameters a = 207.35 A, b = 207.35 A, c = 545.47 A, alpha = 90°, beta = 90°, and gamma = 120°. Assembles to form a 20-nm-diameter particle comprising 60 protein subunits, arranged with 532 symmetry when crystallised at low pH in the presence of phosphate or sulphate ions. Particles form rapidly and are stable in solution during gel filtration at low pH. They are probably formed through trimers of pentamers, which are stabilised by the interaction of two phosphate ions with residues of the N-terminal domains of subunits at the 3fold axis. Once the particles are formed at high concentrations of phosphate (or sulphate), they remain stable in solution at 20fold lower concentrations of the anion. Guest molecules can be trapped within the hollow protein shell during assembly. The C-termini of the subunits are freely accessible on the surface of the protein cage
Escherichia coli K-12
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
active site of MhpD consists of three acidic residues (Glu105, Glu107, and Glu138), which may be involved in coordinating the divalent cation essential for activity
Escherichia coli K-12
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
30000
-
5 * 35000, fusion protein, SDS-PAGE. 5 * 30000, purified protein, SDS-PAGE
Escherichia coli K-12
35000
-
5 * 35000, fusion protein, SDS-PAGE. 5 * 30000, purified protein, SDS-PAGE
Escherichia coli K-12
151000
-
gel filtration-multiangle laser light scattering
Escherichia coli K-12
Purification (Commentary) (protein specific)
Commentary
Organism
by centrifugation and gel filtration
Escherichia coli K-12
Subunits (protein specific)
Subunits
Commentary
Organism
pentamer
5 * 35000, fusion protein, SDS-PAGE. 5 * 30000, purified protein, SDS-PAGE
Escherichia coli K-12
Other publictions for EC 4.2.1.80
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
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)
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705177
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Assembly of a 20-nm protein ca ...
Escherichia coli K-12
J. Mol. Biol.
396
1379-1391
2010
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661714
Wang
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Paraburkholderia xenovorans
FEBS J.
272
966-974
2005
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1
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4
-
5
2
1
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1
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1
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1
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4
1
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4
1
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4
1
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648402
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Pseudomonas sp., Pseudomonas sp. DJ-12
Arch. Pharm. Res.
23
187-195
2000
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1
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6
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J. Bacteriol.
181
1282-1602
1999
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2
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2
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648401
Pollard
Purification, characterization ...
Escherichia coli
Eur. J. Biochem.
251
98-106
1998
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1
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2
1
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1
1
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2
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1
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648400
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238
56-60
1997
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1
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6
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Harayama
-
Physically associated enzymes ...
Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
J. Bacteriol.
171
6221-6228
1989
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1
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19
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2
1
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1
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648397
Kunz
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Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182, Pseudomonas sp.
J. Bacteriol.
148
72-82
1981
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20
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1
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