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Results 1 - 10 of 15 > >>
EC Number Crystallization (Commentary)
Show all pathways known for 2.4.2.7Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.7comparison of the crystal structure of PRPP-Mg2+-bound hAPRT to the ADE/PRPP-Mg2+ and AMP complex structures
Show all pathways known for 2.4.2.7Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.7enzyme complexes phosphate-hAPRT, hypoxanthine-PRPP-Mg2+-hAPRT, IMP-hAPRT, and GMP-hAPRT, mixing of 400 nl of 5 mg/ml protein complexes in 20 mM Tris-HCl, pH 7.4, 5 mM MgCl2, with 200 nl of crystallization solution made of 85 mM Tris-HCl, pH 8.5, 170 mM NaOAc, 19-21% PEG 4000, and 0-30% glycerol, overnight at 20°C, X-ray diffraction structrue determination and analysis at resolution 1.55-1.90 A, molecular replacement using the structure with PDB ID 6FCH as template, and modeling
Show all pathways known for 2.4.2.7Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.7enzyme in complex with adenosine-5'-monophosphate and a phosphate ion, crystallization at 4°C by hanging-drop vapor-diffusion method
Show all pathways known for 2.4.2.7Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.7enzyme, 10 mg/ml, in complex with 9-deazaadenine and sulfate or Mg-phosphoribosyldiphosphate, 50 mM Hepes, pH 6.0, 8 mM MgCl2, 1 mM DTT, 1:2 molar ratio of 9-deazaadenine and iminoribitol, 1 mM sodium diphosphate, after 45 min incubation preparation of crystallization drops, crystals are obtained from mother liquid 0.1 M sodium acetate, pH 4.6, 24% polyethylene glycol 4000, 0.2 M ammonium sulfate, 0.05 M urea, 18°C, X-ray diffraction structure analysis, hydrogen bond network in the complexes
Show all pathways known for 2.4.2.7Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.7four crystal structures: (1) a structure (the enzyme/Pi complex) refined at 2.4 A with inorganic phosphate or sulfate bound in the 5-phosphoribosyl binding pocket, (2) an adenine bound structure (the enzyme/adenine complex) refined at 2.4 A, which shows adenine together with phosphates both at the 5'-phosphoryl and PPi positions of the presumed PRPP binding site, (3) an AMP bound structure (the enzyme/AMP complex) refined at 2.4 A, and (4) an ADP bound structure (the enzyme/ADP complex), refined at 2.8 A containing the inhibitor ADP bound like AMP with both the alpha- and beta-phosphates occupying the 5'-phosphoribosyl binding site. No crystals of the enzyme in complex with 5-phosphoribosyl-alpha-1-pyrophosphate are obtained, likely because the enzyme catalyzes a slow breakdown of 5-phosphoribosyl-alpha-1-pyrophosphate to ribose 5-phosphate and PPi. The crystal structure suggests that the enzyme evolves from a 6-oxopurine phosphoribosyltransferase. The individual subunit adopts an overall structure that resembles a 6-oxopurine phosphoribosyltransferase (PRTase) more than known adenine phosphoribosyltransferases implying that adenine phosphoribosyltransferase functionality in Crenarchaeotae has its evolutionary origin in this family of 6-oxopurine phosphoribosyltransferases. The N-terminal two-thirds of the polypeptide chain folds as a traditional type I PRTase with a five-stranded beta-sheet surrounded by helices. The C-terminal third adopts an unusual three-helix bundle structure that together with the nucleobase-binding loop undergoes a conformational change upon binding of adenine and phosphate resulting in a slight contraction of the active site
Show all pathways known for 2.4.2.7Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.7hanging drop vapour diffusion method, with 15% (v/v) glycerol, 25.5% (w/v) PEG 4000, 0.17 M sodium acetate, and 0.085 M Tris-HCl, pH 8.5
Show all pathways known for 2.4.2.7Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.7mixing of protein solution 13-15 mg/ml with an equal volume of mother liquid 0.1 M Hepes, pH 7.5, 1.5 M lithium sulfate, then equilibration against mother liquid at 18°C, crystals appear after 3 days, X-ray diffraction structure analysis, also crystallization of the enzyme in presence of diphosphate, Mg2+ or inhibitor immucillin, which do not bind at the active site
Show all pathways known for 2.4.2.7Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.7purified His-tagged recombinant enzyme in complex with inhibitors D-DIAB and L-DIAB, and also with adenine, X-ray diffraction structure determination and analysis of enzyme-inhibitor complexes at 1.78 A and 1.98 A resolution, respectively, modeling, structure comparisons
Show all pathways known for 2.4.2.7Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.7purified recombinant enzyme APRT2, hanging-drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 200 mM NaCl and 20 mM Tris-HCl, pH 8.0, with 0.001 ml of precipitant solution containing 19% PEG 20000 and 0.1 M sodium citrate, pH 6.0, 30-50 days, 20°C, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement using the structure of TthAPRT1 from Thermus thermophilus HB8 (PDB ID 1VCH) as a template
Show all pathways known for 2.4.2.7Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.7purified recombinant enzyme in apoform and in complex with substrate adenine, sitting drop vapor diffusion method, mixing of 10 mg/ml protein in 20 mM HEPES, pH 7.5, 150 mM NaCl, 1 mM DTT, and 10% glycerol, with crystallization solutions (a) 0.1 M Tris/HCl pH 8.5, 30% PEG 4000 and 0.2 M MgCl2 and (b) 0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, pH 8.5, 30% PEG 4000, X-ray diffraction structure determination and analysis at 1.9-2.28 A resolution
Results 1 - 10 of 15 > >>