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2.5.1.29: geranylgeranyl diphosphate synthase

This is an abbreviated version!
For detailed information about geranylgeranyl diphosphate synthase, go to the full flat file.

Word Map on EC 2.5.1.29

Reaction

(2E,6E)-farnesyl diphosphate
+
isopentenyl diphosphate
=
diphosphate
 +
geranylgeranyl diphosphate

Synonyms

At4g36810, bifunctional farnesyl/geranylgeranyl diphosphate synthase, BTS1, CcGGDPS1, CcGGDPS2, CotB1, CrtE, DR1395, EgcrtE, EuFPS1, EuFPS2, farnesyl diphosphate/geranylgeranyl diphosphate synthase, farnesyl-diphosphate/geranylgeranyldiphosphate, farnesyltransferase, FPPS/GGPPS, geranylgeranyl diphosphate synthase, geranylgeranyl diphosphate synthase 1, geranylgeranyl diphosphate synthase 11, geranylgeranyl pyrophosphate synthase, geranylgeranyl pyrophosphate synthase GACE1337, geranylgeranyl pyrophosphate synthase GGPPS1-1, geranylgeranyl pyrophosphate synthase GGPPS1-2, geranylgeranyl pyrophosphate synthetase, geranylgeranyl-PP synthetase, geranylgeranyl-pyrophosphate synthase, GGDP synthase, GGDPS, GGPP synthase, GGPP-S, GGPPase, GGPPS, GGPPS 1, GGPPS 191, GGPPS 2, GGPPS 3, GGPPS 595, GGPPS 727, GGPPS1, GGPPS11, GGPS, Ggps1, GGs1, GgsA, GgsB, GGSP1, gps, HpGGPPS, HsGGPPS, IbGGPS, IdsA, isoprenyl diphosphate synthase, leaf-specific geranylgeranyl pyrophosphate synthase, More, PaxG, PfFPPS, PfGGPPS, Saci_0092, short-chain type-III GGPP, synthetase, geranylgeranyl pyrophosphate, TgFPPS, Tk-IdsA, trans-prenyl diphosphate synthase, type II geranylgeranyl diphosphate synthase, type-III geranylgeranyl pyrophosphate synthase, type-III GGPPS

ECTree

     2 Transferases
         2.5 Transferring alkyl or aryl groups, other than methyl groups
             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
                2.5.1.29 geranylgeranyl diphosphate synthase

Crystallization

Crystallization on EC 2.5.1.29 - geranylgeranyl diphosphate synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor-diffusion at 37°C. The three-dimensional structure of determined by X-ray diffraction to 2.5 A resolution
hanging drop method. Structures of a series of n-alkyl and dialkenyl bisphosphonates bound to GGPPS. The binding modes seen crystallographically can be well predicted computationally, facilitating the development of quantitative structure-activity models
native protein, 20°C, sitting drop vapour diffusion mthod, mixing of 200 nl of 90 mg/ml protein in 10 mM HEPES, pH 7.5, 500 mM NaCl, 5% glycerol with 100 nl of precipitant solution consisting of 25% PEG 3350, 200 mM magnesium formate, pH 5.5, and equilibration against 0.1 ml of the precipitant solution, selenomethionine-labeled protein by suspending a 0.003 ml drop containing 26 mg/ml protein, 333 mM NaCl, 0.67 mM MgCl2, 0.67 mM GGPP, 3% glycerol, 15% 2-methyl-2,4-pentanediol, 1.7% PEG 10,000, 6.7 mM HEPES, pH 7.5, over a 1 ml reservoir containing 45% 2-methyl-2,4-pentanediol, and 5% PEG 10000, X-ray diffraction structure determination and analysis at 2.7-2.8 A resolution
-
sitting drop vapor diffusion method at 19°C. 2.2 A crystal structure of hGGPPS in complex with ibandronate
enzyme forms a heterotetramer of two catalytic large plus two regulatory small subunits. No activity is detected for individually expressed large or small subunits
-
hanging-drop vapor-diffusion technique at 20°C. Crystal structure is determined at 2.0 A resolution
purified recombinant GGPPS, in apo form or in complex with zoledronate, hanging drop vapour diffusion method, for the apo enzyme crystals: 0.0015 ml of 16.5 mg/ml protein in 10 mM HEPES, pH 7.5, 500 mM NaCl, is mixed with 0.0015 ml of reservoir solution containing 22% PEG 3350, 200 mM Li2SO4, 100 mM Tris, pH 8.5, for the inhibitor complex crystals: 0.0015 ml of 11.2 mg/ml protein and 10 mM zoledronate, 10 mM IPP, 10 mM MgCl2, 10 mM HEPES, pH 7.5, 500 mM NaCl are mixed with 0.0015 ml reservoir solution containing 20% PEG 3350, 200 mM Li2SO4, 100 mM Tris, 8.5, 18°C, overnight, X-ray diffraction structure determination and analysis at 2.1 A resolution
-
hanging drop method, X-ray crystallographic structures of the N-[methyl(4-phenylbutyl)]-3-aminopropyl-1-hydroxy-1,1-bisphosphonate, bound to geranylgeranyl diphosphate synthase
native and selenomethionine-labeled enzymes, hanging drop vapour diffusion method, mixing of 0.002 ml of the GGPP solution with 10–12 mg/ml protein in 25 mM Tris-HCl, pH 7.5, 150 mM NaCl, and 0.1% Triton X-100 with 0.002 ml of the mother liquor containing 0.08 M CH3COONa, 0.145 M (NH4)2SO4, 13% polyethylene glycol 4000, 7-9% glycerol, and 7-9% 1,2-propanediol, and equilibrating with 0.5 ml of the mother liquor, 7 days room temperature, X-ray diffraction structure determination and analysis at 1.98 A resolution
-
structures of enzyme-inhibitor complexes with isopentenyl diphosphate, geranyl diphosphate, farnesyl diphosphate, geranylgeranyl diphosphate, zoledronate, minodronate, BPH-629, BPH-364, and BPH-675
the 3D structure of GGPPS reveals an unique positioning of the N-terminal helix A, which protrudes into the other subunit and stabilizes dimerization, although it is far from the main dimer interface. The replacement of residues L8 and I9 at this helix with Gly is sufficient to disrupt the dimer into a monomer, leading to at least 1000fold reduction in activity
purified recombinant wild-type of selenomethionine-labeled enzyme, 20 mg/mL protein in 10 mM Tris-HCl, pH 7.9, 10 mM MgCl2, 100 mM NaCl, and 0.5 mM tris(2-carboxyethyl)phosphine, crystals of SeMet-labeled enzyme are obtained by vapor diffusion with hanging drops that contain a 1:1 mixture of protein solution and reservoir buffer D, the latter containing 100 mM sodium acetate, pH 4.4, 40% v/v propanediol, 10 mM MgCl2, and 0.5 mM TCEP, liquid nitrogen freezing without the addition of a cryo protectant, a second crystal form is obtained with native enzyme using the same procedure but with reservoir buffer E containing 100 mM N-cyclohexyl-3-aminopropane sulfonic acid, pH 10.0, 200 mM NaCl, 9-11% PEG 8000, 10 mM MgCl2, and 0.5 mM TCEP, mixing with reservoir buffer E containing 30% v/v glycerol and flash-freezing in liquid nitrogen, X-ray diffraction structure determination and analysis at 1.8-2.0 A resolution, multiwavelength anomalous diffraction, soaking of native enzyme with FPP and Mg2+ fails, overview
sitting drop vapor diffusion method at 16°C. The crystal structure of CrtE solved to a resolution of 2.7 A reveals a strong structural similarity to the large subunit of the heterodimeric geranylgeranylpyrophosphate synthase 1 from Arabidopsis thaliana with each subunit containing 14 helices
sitting drop vapor diffusion method at 16°C. The crystal structure of CrtE solves to a resolution of 2.7 A. Strong structural similarity to the large subunit of the heterodimeric geranylgeranyl pyrophosphate synthase 1 from Arabidopsis thaliana with each subunit containing 14 helices
as recombinant native protein and as selenomethionine derivative, sitting-drop vapour-diffusion method, well diffracting crystals are obtained belonging to the tetragonal space group P4(1) or P4(3) with unit-cell paramaters a = b = 139.88, c = 73.37 A. there are two homodimers in the asymmetric unit
-