2.5.1.31: ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]
This is an abbreviated version!
For detailed information about ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific], go to the full flat file.
Word Map on EC 2.5.1.31
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2.5.1.31
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isoprenoids
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cis-prenyltransferase
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prenyltransferases
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dolichols
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luteus
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dhdds
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trans-prenyltransferases
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pharmacology
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octaprenyl
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drug development
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medicine
- 2.5.1.31
-
isoprenoids
- cis-prenyltransferase
- prenyltransferases
- dolichols
- luteus
- dhdds
- trans-prenyltransferases
- pharmacology
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octaprenyl
- drug development
- medicine
Reaction
Synonyms
bactoprenyl-diphosphate synthase, C55-OO synthetase, C55PP synthetase, cis,polyprenyl diphosphate synthase, cis-prenyl chain elongating enzyme, cis-type undecaprenyl pyrophosphate synthase, CPDS, DDPPs, dehydrodolichyl diphosphate synthase, di-trans,poly-cis-decaprenylcistransferase, di-trans,poly-cis-undecaprenyl-diphosphate synthase, di-trans-poly-cis-decaprenyl cistransferase, isosesquilavandulyl diphosphate synthase, Mcl22, More, synthetase, undecaprenyl pyrophosphate, undecaprenyl diphosphate phosphatase, undecaprenyl diphosphate synthase, undecaprenyl diphosphate synthetase, undecaprenyl pyrophosphate synthase, undecaprenyl pyrophosphate synthetase, undecaprenyl-diphosphate synthase, undecaprenyl-pyrophosphate synthase, UPP synthase, UPP synthetase, UPP, C55 synthase, UPPs, UPS, Z-prenyl diphosphate synthase
ECTree
2.5.1.31 ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]Advanced search results
results (
results (Crystallization
Crystallization on EC 2.5.1.31 - ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion method. Cocktailed fragment screening by X-ray crystallography
in complex with farnesyl diphosphate. Virtual screening of inhibitors from a library of 58,635 compounds, modelling of inhibitors N,N'-bis(6-chloro-1,3-benzothiazol-2-yl)methanedisulfonamide and 3-[5-(5,6-dihydrobenzimidazo[1,2-c]quinazolin-6-yl)-2,5-dihydrofuran-2-yl]benzenesulfonamide into structure
purified His-tagged wild-type enzyme in complex with Mg2+, sulfates, and 2 molecules of Triton X-100, hanging drop vapour diffusion method, 0.002 ml protein solution containing 10 mg/ml protein, 2% Triton X-100, 5 mM MgCl2, and 0.66 mM farnesyl diphosphate, is mixed with equal volume of mother liquid containing 0.01 M CoCl2, 0.1 M MES, pH 6.5, and 1.8 M ammonium sulfate, equilibration against 0.2 ml mother liquid at 25°C, 10 days, X-ray diffraction structure determination and analysis at 1.73 A resolution, modeling
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purified His-tagged wild-type enzyme, hanging drop vapour diffusion method, high concentration of sulfate or phosphate in the mother liquid to prevent binding of Triton X-100 or substrates during crystallization, 0.002 ml mother liquid containing 25% ethylene glycol, pH 7.5, mixed with 0.002 ml protein solution containing 10 mg/ml protein, 1 mM peptide, 0.05% Triton X-100, and 0.5 mM MgCl2, equilibration against 0.2 ml mother liquid at 25°C, 5 days, crystals are then soaked in mother liquid containing 0.23 mM farnesyl diphosphate, X-ray diffraction structure determination and analysis at 2.4 A resolution, modeling
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purified recombinant His-tagged enzyme in complex with inhibitor clomiphene, sitting drop vapor diffusion in the presence or absence of 1 mM clomiphene using a reservoir solution of 100 mM MES, pH 6.5, 0.16 M calcium acetate, 20% PEG 8000, 20% glycerol (+ clomiphene) or 0.1 M lithium sulfate, 0.1 M ADA 6.5, 12% w/v PEG 4000, 20% glycerol (-clomiphene), X-ray diffraction structure determination and analysis at 2.15 A resolution, molecular replacement using structure PDB ID 1X06 as a search model
purified recombinant wild-type and mutant D26A enzymes in complex with Mg2+, isopentenyl diphosphate and substrate analogue farnesyl thiodiphosphate, protein solution containing 10 mg/ml protein in 25 mM Tris-HCl, pH 7.5, 150 mM NaCl, and 0.03% Triton X-100, is mixed with dried MgCl2 and isopentenyl diphosphate powder, hanging drop vapour diffusion method, 0.002 ml of the final protein solution with equal volume of mother liquor containing 20% ethylene glycol, 2-5% PEG 35000, equilibration against 0.5 ml mother liquor at room temperature, 2 days, soaking in cryoprotectant containing 2.5 mM MgCl2, 2.5 mM isopentenyl diphosphate, 30% ethylene glycol, and 5% PEG 35000 for 1 day, X-ray diffraction strcture determination and analysis at 1.9-2.2 A resolution, molecular modeling
C234A UPPS mutant to prevent intra-molecular disulfide bond formed during the long period of crystallization process is crystallized using the hanging drop method. The protein is a dimer and each subunit contains a catalytic domain and a pairing domain. Two subunits are tightly associated through the central beta-sheet and a pair of long alpha-helices. Helicobacter pylori UPPS has a 1.5-turn shorter alpha5 helix in the dimer interface. This may weaken the dimer formation for Helicobacter pylori UPPS. The catalytic domain is composed of six beta-strands and four beta-helices and the central tunnel-shaped active site is surrounded by 2 alpha-helices and 4 beta-strands
crystal structure of Helicobacter pylori UPPS and mutant by hanging drop method
in complex with farnesyl diphosphate. Virtual screening of inhibitors from a library of 58,635 compounds, modelling of inhibitors N,N'-bis(6-chloro-1,3-benzothiazol-2-yl)methanedisulfonamide and 3-[5-(5,6-dihydrobenzimidazo[1,2-c]quinazolin-6-yl)-2,5-dihydrofuran-2-yl]benzenesulfonamide into structure
sitting-drop vapour-diffusion method with ammonium sulfate and lithium sulfate as precipitants
the crystal structure is used for moelling with bound inhibitor tetramic acid
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the overall structure is determined at 2.2 A resolution by multiple isomorphous replacement with anomalous scattering
purified recombinant enzyme free or in complex with substrate (2E,6E)-farnesyl diphosphate, X-ray diffraction structure determination and analysis at resolutions of 2.2 A and 2.1A, respectively
apoenzyme and enzyme bound to dimethylallyl diphosphate, geranyl diphosphate and dimethylallyl diphosphate plus S-thiologeranyl diphosphate
