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Results 1 - 5 of 5
EC Number Crystallization (Commentary)
Show all pathways known for 2.5.1.90Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.90mutants A76Y, A76Y/S77F, F132A/L128A, F132A/L128A/I123A, and F132A/L128A/I123A/D62A to 3.1, 2.7, 3.3, 3.35 and 3.4 A resolution, respectively. Like wildtype OPPs, all mutant structures contain 12 alpha-helices, nine of them surrounding a large central cavity and an elongated tunnel-shaped active site cavity surrounded by four alpha-helices In the crystal structure of the A76Y/S77F mutant, F77 is pushed away by Y76, thereby creating more space between those two large amino acids to accommodate the C20 product. A large F132 residue at the bottom of the tunnel-shaped active site serves as the floor and determines the final product chain length. The substitution of F132 with a small Ala, thereby removing the blockade, leads to the synthesis of a C50 product larger than that produced by the wild-type enzyme
Show all pathways known for 2.5.1.90Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.90native enzyme and selenomethionine derivative, to 2.0 A and 2.8 A resolution, respectively. Residues Arg87, Lys36 and Arg39 are essential for isopentenyl diphosphate binding. Residues Lys162, Lys224 and Gln197 are involved in farnesyl diphosphate binding. The second DDXXD motif may be involved in farnesyl diphosphate binding by Mg2+-mediated interactions, Leu127 is probably involved in product chain length determination and the intermediate products such as geranylgeranyl diphosphate need a rearrange to occupy the binding site of farnesyl diphosphate and then isopentenyl diphosphate is reloaded
Show all pathways known for 2.5.1.90Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.90purified recombinant enzyme, crystallization method screening, sitting drop vapour diffusion method, mixing of 0.002 ml of 3 mg/ml protein in 25 mM Tris-HCl, 150 mM NaCl, pH 7.5, with 0.002 ml of crystallization solution containing 0.3 M magnesium chloride hexahydrate, 0.1 M Tris-HCl, pH 8.5, 24% w/v PEG 3350, 3-4 days, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement, the crystal contains one homodimer per asymmetric unit, structure modelling
Show all pathways known for 2.5.1.90Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.90purified recombinant His-tagged enzyme in apo-form and in complexes with isopentenyl diphosphate and a farnesyl diphosphate thio-analogue, FsPP, sitting drop vapor diffusion method, mixing of 0.002 ml of 3 mg/ml protein in 25 mM Tris-HCl, pH 7.5, and 150 mM NaCl, with 0.002 ml of reservoir solution containing 0.3 M magnesium chloride, 0.1 M Tris-HCl, pH 8.5, and 24% w/v PEG 3350, and equilibration against 0.3 ml of reservori solution, 22°C, 3-4 days, X-ray diffraction structure determination and analysis at resolutions of 2.2-2.6 A
Show all pathways known for 2.5.1.90Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.90wild-type and mutants F52A, V73A, S77F, F132A, to 2.28, 2.80, 2.85, 2.45 and 2.40 A resolution, respectively. OPPs is composed entirely of alpha-helices joined by connecting loops and is arranged with nine core helices around a large central cavity. An elongated hydrophobic tunnel between D and F alpha-helices contains two DDXXD motifs on the top for substrate binding and is occupied at the bottom with two large residues Phe-52 and Phe-132
Results 1 - 5 of 5