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5.4.99.5: chorismate mutase

This is an abbreviated version!
For detailed information about chorismate mutase, go to the full flat file.

Word Map on EC 5.4.99.5

Reaction

chorismate
=
prephenate

Synonyms

105-MtCM, 90-MtCM, AmtCM1, AmtCM2, aro7, AroA, AroH, AroQ, AtCM1, AtCM2, AtCM3, Bacillus subtilis chorismate mutase, Bphy_7813, BsAroH, BsCM, BsCM_2, BTH_I1596, chorismate mutase, chorismate mutase 1, chorismate mutase-prephenate dehydrogenase, Chorismate mutase/prephenate dehydratase, CM, CM type 2, CM-1, CM-prephenate dehydratase, CM-TyrAp, CM/PDT, CM/PDT/PDHG, CM0819, CM1, CM2, EcCM, EcCM-R, MI-CM-1, MI-CM-2, MjCM, MTB chorismate mutase, MTB CM, MtbCM, MtCM, Mutase, chorismate, Mycobacterium tuberculosis chorismate mutase, Mycobacterium tuberculosis H37Rv chorismate mutase, NC30, P protein, P-protein, PheA, PpCM1, PpCM2, Rv0948c, Rv1885c, SmCM, Tparo7, TtCM, y2828, YCM

ECTree

     5 Isomerases
         5.4 Intramolecular transferases
             5.4.99 Transferring other groups
                5.4.99.5 chorismate mutase

Crystallization

Crystallization on EC 5.4.99.5 - chorismate mutase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant detagged wild-type enzyme in complex with phenylalanine or tyrosine, hanging drop vapordiffusion method, mixing 0f 0.001 ml of 9 mg/ml protein in 25 mM HEPES, pH 7.5, and 100 mM NaCl, with 0.001 ml of reservoir solution containing 30% PEG 400, 0.1 M HEPES, pH 7.5, 0.2 M MgCl2, and 1 mM of either phenylalanine or tyrosine, X-ray diffraction structure determination and analysis at 2.30-2.45 A resolution, molecular replacement using yeast chorismate mutase structure, PDB ID 4CSM, as a search model
crystal structures of double mutants C88S/R90K and C88K/R90S, hanging drop vapour diffusion method at room temperature, space group R3 with a and b: 82.6 A and c: 42.8 A
hanging drop vapor-diffusion method at room temperature and high ionic strength, orthorhombic space group P212121 with a: 52.2 A, b: 83.8 A, c: 86.0 A, nine sulfate ions, five glycerol molecules, 424 water molecules
Performance of molecular dynamics simulations for the three enzyme-ligand complexes(CHOR,PRE and TSA) in addition to the TPS calculations. 8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid as a TSA. The principal component analysis (PCA) to analyze structures is used
purified recombinant enzyme AroQ (BsCM_2) in complex with citrate and chlorogenic acid, sitting drop vapor diffusion method, mixing of 0.001 ml of 18 mg/ml protein in 25 mM Tris-HCl, pH 7.5, and 50 mM NaCl, with 0.001 ml of reservoir solution containing 1 M ammonium sulphate, 0.1 M potassium sodium tartrate, and 0.1 M sodium citrate, pH 5.8, 20°C, 15 days, X-ray diffraction structure determination and analysis at 1.9 A and 1.8 A resolution, respectively, molecular replacement using the structure of the N-terminal CM domain of bifunctional DAHPS from Listeria monocytogens (PDB ID 3NVT) as template
purified recombinant wild-type enzyme, hanging drop vapor diffusion technique, mixing of 0.001 ml of 3 mM protein in 10 mM Tris buffer, pH 7.5, 2 mM DTT, and 0.125 mM EDTA with 0.001 ml of reservoir solution containing 100 mM malic acid, Mes, Tris (MMT buffer) (in molar ratios of 1:2:2, respectively), pH 6.0, 100-150 mM MgCl2, 25% w/v PEG 1000, and 0.3 mM NaN3, at 20°C, 4-5 days, X-ray diffraction structure determination and analysis at resolution at 1.59 A resolution, molecular replacement using crystal structure PDB ID 1DBF as search model. Purified recombinant mutant enzyme Arg90Cit free or complexed with either substrate, product, or a transition state analogue, hanging drop vapor diffusion technique, mixing of 750 nl of 3 mM protein in 20 mM Tris, pH 8.0, 0.6 mM PMSF, 0.3 mM NaN3 with 750 nl of reservoir solution 100 mM MMT buffer pH 6.0, 50-150 mM CaCl2, 24-26% w/v PEG 1000, and 0.3 mM NaN3, at 20°C, 3-4 days, X-ray diffraction structure determination and analysis at resolution at 1.61-1.80 A resolution, modeling
structure of N-terminal domain AroQ in complex with citrate and chlorogenic acid at 1.9 A and 1.8 A resolution, respectively. Helix H2' undergoes uncoiling at the first turn and increases the mobility of loop L1'. The side chains of Arg45, Phe46, Arg52 and Lys76 undergo conformational changes, which may play an important role in DAHPS regulation by the formation of the domain-domain interface. Chlorogenic acid binds with a higher affinity than chorismate
purified recombinant enzyme, sitting drop vapor diffusion method, mixing of 400 nl of 20 mg/ml protein in 20 mM HEPES, pH 7.0, 300 mM NaCl, 5% glycerol, and 1 mM TCEP, with 400 nl reservoir solution containing 20% w/v PEG 3350, 200 mM ammonium nitrate, and equilibration against 0.08 ml of reservoir solution, 17°C, X-ray diffraction structure determination and analysis at 2.15 A resolution
*MtCM, encoded by ORF Rv1885c in strain H37Rv. First characterized example of an AroQgamma fold. Description of the crystal optimization of a protein target that crystallizes very rapidly. 1. 175-residue version of *MtCM (encoded on plasmid pKTU3-HCT, dissolved in 20 mM potassium phosphate buffer pH7.5. 2. leaderless untagged 167-residue version of *MtCM encoded by plasmid pKTU3-HT used, buffered with 20 mM Tris-HCl pH 8.0)
37.2 kDa. Each asymmetric unit contains a homodimer, corresponding to the two protomers of the biological dimer. *MtCM as a model system for the *AroQ subclass and determined its crystal structure at high resolution, both in its unliganded form and in complex with transition state analog (1S,3S,5R,6R)-6-hydroxy-4-oxabicyco[3.3.1]non-7-ene-1,3-dicarboxylic acid. Heavy-atom derivatives prepared. Successful heavy-atom compounds are lead (II) acetate and thallium (III) acetate
alone and in complex with 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase, hanging drop vapor diffusion method, using 25% (w/v) PEG 1500 and 0.1 M MMT buffer (L-malic acid, MES, Tris) pH 8.0-9.0
Analysis of the structure shows a novel fold topology for the protein with a topologically rearranged helix containing R134. *MtCM does not have an allosteric regulation site
analysis reveals the presence of two monomers in the asymmetric unit
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in complex with L-malate, hanging drop vapor diffusion method, using 15% (w/v) PEG 1500 and 0.1 M of the L-malate-containing MMT buffer system pH 8.0-9.0
MtCM (Rv1885c) (PDB ID-2F6L), docked conformation of (3S,6Z)-8-hydroxy-2-oxabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid, 4-[[2-(3,4-dimethoxyphenyl)ethyl]amino]-3-nitro-5-sulfamoylbenzoic acid, and (3S,6Z)-8-hydroxy-2-azabicyclo[3.3.3]undec-6-ene-3,5-dicarboxylic acid, (2Z)-2-(4-chlorophenyl)-3-(4,5-dimethoxy-2-nitrophenyl)prop-2-enoic acid in the catalytic site of MtCM x-ray crystal structure is shown
of the homodimeric chorismate mutase (Rv1885c). The crystal structure corresponds to the AroQ class CM of Mycobacterium tuberculosis. Determination of the crystal structure of the unique extracytoplasmic MtbCM in complex with its allosteric ligand, L-Trp. Se-Met MtbCM crystallizes in space group C2 in the presence of Trp. The Mycobacterium tuberculosis enzyme is an all-helical protein. Structural comparisons show that CMs from different organisms have envolved into two completely unrelated protein folds, suggesting separate evolutionary origins of the enzyme. On the basis of the structural fold adopted by the protein, CMs have been classified into the AroH and AroQ classes
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sitting drop vapour diffusion method, using 0.1 M Tris-HCl (pH 8.6), 0.2 M MgCl2, and 20% poly(ethylene glycol) 400 for the 90 amino acid enzyme 90-MtCM
purified recombinant enzyme, sitting drop vapor diffusion method, mixing of 400 nl of 22.4 mg/ml protein in 20 mM HEPES, pH 7.0, 300 mM NaCl, 5% glycerol, and 1 mM TCEP, with 400 nl reservoir solution containing 20% w/v PEG 3350, 200 mM ammonium formate, pH 6.6, and equilibration against 0.08 ml of reservoir solution, X-ray diffraction structure determination and analysis at 1.95 A resolution
purified recombinant detagged isozyme PpCM1 in complex with tryptophan, hanging drop vapor diffusion method, mixing of 0.001 ml of 6 mg/ml proteinin 25 mM HEPES, pH 7.5, and 100 mM NaCl with 0.001 ml of reservoir solution containing 10% w/v PEG 4000, 20% v/v 2-propanol, and 100 mM HEPES, pH 7.5, at 4°C, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement using Arabidopsis thaliana isozyme AtCM1 in complex with tyrosine structure (PDB ID 4PPU) as search model, modeling
crystal structure of the T state of the allosteric enzyme and comparison with the R state
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crystal structure of wild-type enzyme cocrystallized with Trp and an endo-exabicyclic transition state analogue inhibitor, of wild-type enzyme cocrystallized with Tyr and the endo-oxabicyclic transition state analogue inhibitor and of the Thr226Ser mutant enzyme in complex with Trp
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Thr226Ile mutant enzyme
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The corresponding positional fluctuations from the MD simulation are in good agreement with those obtained by X-ray crystallography
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hanging drop vapour diffusion method, in 2 M ammonium sulfate, 0.1 M citrate/phosphate buffer, pH 4.2