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heterodimer
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x-ray crystallography
tetramer
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4 * 47000, chorismate mutase/prephenate dehydratase, SDS-PAGE
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x * 40000, the smallest native species of the enzyme, determined by sedimentation equilibrium, appears to be a dimer
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x * 40000, chorismate mutase/prephenate dehydratase, tryptic fingerprinting suggests that the 40000 MW subunits are closely similar if not identical
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x * 14500, at least 3 subunits not linked together by disulfide bridges, SDS-PAGE
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x * 14500, at least 3 subunits not linked together by disulfide bridges, SDS-PAGE
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?
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two different components are detected by gel filtration, component A with MW 250000 and component B with MW 25000. The two components associate reversibly to give an active enzyme complex with MW 320000
dimer
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2 * 45000, SDS-PAGE
dimer
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2 * 14500, SDS-PAGE
dimer
in the BsCM_2-chlorogenic acid structure, two active sites, S1 and S2, are located at the interface of two monomers
dimer
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in the BsCM_2-chlorogenic acid structure, two active sites, S1 and S2, are located at the interface of two monomers
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dimer
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2 * 39000, SDS-PAGE
dimer
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2 * 42042, calculation from nucleotide sequence
dimer
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SDS-PAGE and gel filtration
dimer
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the dimeric chorismate mutase is a thermostable and conventionally folded enzyme, X-ray chrystallography
dimer
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2 * 22000, gel filtration, SDS-PAGE
dimer
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alpha2, ultracentrifugation, gel filtration
dimer
Each assymmetric unit contains a homodimer, corresponding to the two protomers (A and B) of the biological dimer. The structure of a *MtCM protomer strongly resembles the fold of the EcCM dimer, which consists of two intertwined subunits of three helices each and which comprises two active sites
dimer
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alpha2, ultracentrifugation, gel filtration
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dimer
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Each assymmetric unit contains a homodimer, corresponding to the two protomers (A and B) of the biological dimer. The structure of a *MtCM protomer strongly resembles the fold of the EcCM dimer, which consists of two intertwined subunits of three helices each and which comprises two active sites
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homodimer
2 * 28000-30000, recombinant detagged enzyme, SDS-PAGE
homodimer
2 * 32600, recombinant enzyme, SDS-PAGE
homodimer
Q9Y7B2
alpha2, 2 * 30000, calculated from amino acid sequence, homology modeling, electron microscopy
homodimer
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2 * 12000, SDS-Page
homodimer
alpha2, 2 * 11883-11887, deduced from amino acid sequence, ESI-MS, MALDI-MS
homodimer
recombinant enzyme, low-temperature SDS-PAGE
homodimer
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alpha2, 2 * 12843-12848, deduced from amino acid sequence, ESI-MS, MALDI-MS
homodimer
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native enzyme
homodimer
2 * 18747, all alpha-helical bundle structure, two monomeric subunits
homodimer
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The regulating Trp ligand is found to be sandwiched between the two monomers in a dimer containing residues 66-68
homodimer
2 * 6000, SDS-PAGE
homodimer
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2 * 18747, all alpha-helical bundle structure, two monomeric subunits
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homodimer
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2 * 6000, SDS-PAGE
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homodimer
2 * 28000-30000, recombinant detagged enzyme, SDS-PAGE
homodimer
2 * 28000-30000, recombinant detagged enzyme, SDS-PAGE
homodimer
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2 * 19000, SDS-PAGE
homodimer
x-ray crystallography
homohexamer
6 * 66000, SDS-PAGE
homohexamer
6 * 70946, calculated from sequence
monomer
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monomeric chorismate mutase combines high catalytic activity with the characteristics of a molten globule, X-ray crystallography
monomer
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provides essentially the same catalytic power as the native enzyme, behaves like a molten globule (an ensemble of poorly packed and rapidly interconverting conformers)
trimer
alpha3, crystallization studies
trimer
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crystal structure
trimer
alpha3, 3 * 15800, SDS-PAGE
trimer
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constisting of three pseudo-alpha/beta barrels
additional information
the high-resolution structure of chorismate mutase is determined in the monoclinic space group P21 with three homodimers per asymmetric unit. The overall structure of each protomer has the prototypical AroQgamma topology and shares conserved binding-cavity residues with other chorismate mutases. The AroQgamma topology is composed entirely of helices connected by short loops
additional information
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the high-resolution structure of chorismate mutase is determined in the monoclinic space group P21 with three homodimers per asymmetric unit. The overall structure of each protomer has the prototypical AroQgamma topology and shares conserved binding-cavity residues with other chorismate mutases. The AroQgamma topology is composed entirely of helices connected by short loops
additional information
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the high-resolution structure of chorismate mutase is determined in the monoclinic space group P21 with three homodimers per asymmetric unit. The overall structure of each protomer has the prototypical AroQgamma topology and shares conserved binding-cavity residues with other chorismate mutases. The AroQgamma topology is composed entirely of helices connected by short loops
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additional information
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In MtbCM, while one face of helix 3 contributes to residues involved in monomer-monomer contracts and the allosteric site, the other face contributes to residues involved in the interaction with the substrate. The active site in the gene duplicated monomer is occupied by a sulfate ion and is located in the second half of the polypeptide
additional information
Ligand-induced structural changes are shown. Experiments neither show evidence for an equilibrium between the dimer and a *MtCM dimer of an intertwined nature, nor for an equilibrium with a monomer at lower protein concentrations as observed for engineered topology variants of chorismate mutases. The active site of *MtCM is highly similar to the catalytic sites of the other structurally characterized AroQ chorismate mutases
additional information
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Ligand-induced structural changes are shown. Experiments neither show evidence for an equilibrium between the dimer and a *MtCM dimer of an intertwined nature, nor for an equilibrium with a monomer at lower protein concentrations as observed for engineered topology variants of chorismate mutases. The active site of *MtCM is highly similar to the catalytic sites of the other structurally characterized AroQ chorismate mutases
additional information
secretory isozyme MtbCM undergoes dimerization mediated through residues (90-119) spanning H3 in both subunits, with the two helices placed anti parallel to each other. The polypeptide consists of eight a-helices H-H8 connected by turns and loop segments
additional information
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secretory isozyme MtbCM undergoes dimerization mediated through residues (90-119) spanning H3 in both subunits, with the two helices placed anti parallel to each other. The polypeptide consists of eight a-helices H-H8 connected by turns and loop segments
additional information
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secretory isozyme MtbCM undergoes dimerization mediated through residues (90-119) spanning H3 in both subunits, with the two helices placed anti parallel to each other. The polypeptide consists of eight a-helices H-H8 connected by turns and loop segments
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additional information
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Ligand-induced structural changes are shown. Experiments neither show evidence for an equilibrium between the dimer and a *MtCM dimer of an intertwined nature, nor for an equilibrium with a monomer at lower protein concentrations as observed for engineered topology variants of chorismate mutases. The active site of *MtCM is highly similar to the catalytic sites of the other structurally characterized AroQ chorismate mutases
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additional information
the enzyme is a chorismate mutases with AroQgamma topology
additional information
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the enzyme is a chorismate mutases with AroQgamma topology
additional information
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the enzyme is a chorismate mutases with AroQgamma topology
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additional information
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enzyme structure comparisons of isochorismate-pyruvate lyase, PchB, with chorismate mutases, overview