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2.5.1.10: (2E,6E)-farnesyl diphosphate synthase

This is an abbreviated version!
For detailed information about (2E,6E)-farnesyl diphosphate synthase, go to the full flat file.

Word Map on EC 2.5.1.10

Reaction

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

Synonyms

At4g36810, bifunctional farnesyl/geranylgeranyl diphosphate synthase, E-farnesyl diphosphate synthase, E-FPP synthase, ERG20, farnesyl diphosphate synthase, farnesyl diphosphate synthase 1, farnesyl diphosphate synthase 2, farnesyl pyrophosphate synthase, farnesyl pyrophosphate synthetase, farnesyl-diphosphate synthase, farnesylpyrophosphate synthetase, FDPSase, FDS, FPP synthase, FPP-synthase, FPPase, FPPS, FPPS/GGPPS, FPPS1, FPPS2, FPPS3, FPS, Fps1, FPS2, geranyl transferase I, geranyltranstransferase, GGPPS11, hFPPS, HpGGPPS, IspA, LS1, MpFPPS1, MpFPPS2, omega,E,E-farnesyl diphosphate synthase, omega,E,E-FPP, PA4043, PcIDS1, prenyltransferase, type I farnesyl diphosphate synthase

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)
                2.5.1.10 (2E,6E)-farnesyl diphosphate synthase

Crystallization

Crystallization on EC 2.5.1.10 - (2E,6E)-farnesyl diphosphate synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular dynamics simulations for wild-type and mutants Q107E, L110W, Q107F, Q107F/L110A, L110A
molecular modeling of structure based on PDB file 1FPS
-
microbatch-under-oil method, crystal structures of apoenzyme, ligand-bound enzyme, and inhibitor-bound structures
sitting-drop vapor diffusion method, crystal structure of FPPase from Geobacillus stearothermophilus is determined at 2.31 A resolution
crystallization of human enzyme from a solution of racemic [6,7-dihydro-5H-cyclopenta[c]pyridin-7-yl(hydroxy)methylene]bis(phosphonic acid) results in a complex containing the R enantiomer in the enzyme active site. Contrary to known complexes of enzyme with risedronate, zoledronate, and minodronate, the complex with [6,7-dihydro-5H-cyclopenta[c]pyridin-7-yl(hydroxy)methylene]bis(phosphonic acid) displays only one Mg2+ ion
hanging drop vapor diffusion method, using 1.2 M phosphate buffer (pH 5.0), 25% (v/v) glycerol
in complex with chiral risedronate analog, [6,7-dihydro-5H-cyclopenta[c]pyridin-7-yl(hydroxy)methylene]bis(phosphonic acid), i.e. NE-10501. The complex contains the R enantiomer in the enzymic active site, which is confirmed by docking studies. Presence of one Mg2+
vapor diffusion in sitting drops. In order to examine the actual binding interactions between the new PNP-BPs and hFPPS, co-crystal structures with the key inhibitors YS05035, JDS05119, and JDS05120 are determined
vapour diffusion in a sitting drop at 22°C. Crystalized in the presence of farnesyl diphosphate, and its X-ray structure is determined at 1.9 A resolution
crystals of mutant enzymes E97Y, T164Y, and T164W, are produced using the hanging drop vapor diffusion technique at 18°C. Proteins are co-crystallized with inhibitor 476A and substrate IPP in the presence of MgCl
hanging drop vapor diffusion technique at 18°C. Crystal structures of mutant enzymes E97Y, T164W, and T164Y bound with 3-butyl-1-(2,2-diphosphonoethyl)pyridinium, isopentenyl diphosphate, and modeled farnesyl diphosphate provide strong evidence that these mutations produce the observed effects by altering the size of the binding pocket for the growing isoprenoid chain in the active site of the enzyme
in complex with isopentenyl diphosphate and inhibitors, hanging drop vapor diffusion method, using 15-25% (w/v) PEG 3350, 0.1-0.2 M calcium acetate, 0.1 M MES sodium salt pH 6.5
-
in complex with natural substrates and inhibitors, sitting drop vapor diffusion method, using 20% (w/v) PEG 3350, 0.2 M NaF, 0.1 M bis-Tris propane pH 6.5
in complex with Mg2+ and inhibitors, vapor diffusion method, using 100 mM sodium acetate, pH 4.6-5.2, 200 mM ammonium sulfate, and 2-10% (w/v) PEG 4K
-
in complex with substrate isopentenyl diphosphate and five nitrogen-containing bisphosphonate inhibitors. The C1-hydroxyl and the nitrogen-containing groups of the inhibitors alter the binding of isopentenyl diphosphate and the conformation of residues Y94 and Q167. binding of the inhibitors changes the binding properties of the second site of the dimer