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Results 1 - 10 of 11 > >>
EC Number Crystallization (Commentary)
Show all pathways known for 6.4.1.2Display the word mapDisplay the reaction diagram Show all sequences 6.4.1.2-
Show all pathways known for 6.4.1.2Display the word mapDisplay the reaction diagram Show all sequences 6.4.1.2carboxyl transferase domain
Show all pathways known for 6.4.1.2Display the word mapDisplay the reaction diagram Show all sequences 6.4.1.2crystal structure of Escherichia coli biotinylated biotin carboxyl carrier protein (BCCP) complexed with biotin carboxylase (BC) to a resolution of 2.49 A. The protein-protein complex shows a unique quaternary structure and two distinct interfaces for each biotinylated biotin carboxyl carrier protein monomer
Show all pathways known for 6.4.1.2Display the word mapDisplay the reaction diagram Show all sequences 6.4.1.2crystal structure of humanized mutant of yeast CT (yCT-H9) in complex with a human ACC2-selective small molecule inhibitor is determined
Show all pathways known for 6.4.1.2Display the word mapDisplay the reaction diagram Show all sequences 6.4.1.2crystallization of the carboxyltranferase domain CT in complex with CoA, inhibitor CP-640186, or herbicides haloxyfop or diclofop
Show all pathways known for 6.4.1.2Display the word mapDisplay the reaction diagram Show all sequences 6.4.1.2enzyme CT domain in complex with inhibitor tepraloxydim, hanging drop vapour diffusion method, at 4°C, 10 mg/ml protein in solution containing 0.1 M sodium citrate, pH 7.5, 8% w/v PEG 8000, 10% v/v glycerol, 5 mM tepraloxydim, and 5% v/v dimethyl sulfoxide, is mixed with reservoir solution containing 0.1 M sodium citrate, pH 5.5,8% w/v PEG 8000, and 10% v/v glycerol, X-ray diffraction structure determination and analysis at 2.3 A resolution
Show all pathways known for 6.4.1.2Display the word mapDisplay the reaction diagram Show all sequences 6.4.1.2purified recombinant carboxyltransferase domain comprising residues 1476-2233 in complex with CP-640186, hanging drop vapour diffusion method, crystallization of the free enzyme in a 10 mg/ml solution using a reservoir solution containing 0.1 M sodium citrate, pH 5.5, 0.2 M NaCl, 8% w/v PEG 8000, and 10% v/v glycerol, soaking of the crystals in 1 mM inhibitor CP-640186, X-ray diffraction structure determination and analyis at 2.8 A resolution
Show all pathways known for 6.4.1.2Display the word mapDisplay the reaction diagram Show all sequences 6.4.1.2purified selenomethionyl biotin carboxylase domain free and with bound inhibitor soraphen A, sitting drop vapour diffusion method for crystallization of free enzyme: 4°C, the reservoir solution contains 0.1 M Bis-Tris propane, pH 6.0, 23% w/v PEG 3350, 0.2 M NaCl, 0.4 M MgCl2, and 5% glycerol, 12-18 days, followed by microseeding, which is essential, sitting drop vapour diffusion method for crystallization of inhibitor-bound enzyme: 50 mg/ml protein are incubated with 0.88 mM soraphen A at 4°C for 1 h prior to crystallization, the reservoir solution for crystallization at 22°C contains 0.1 M Bis-Tris, pH 5.8, 26% w/v PEG 3350, 0.1 M NaCl, 0.2 M MgCl2, 8% glycerol, and 2 mM DTT, as for the free enzyme microseeding is essential, X-ray diffraction structure determination and analysis at 1.8-2.9 A resolution, selenomethionyl multiwavelength anomalous diffraction method
Show all pathways known for 6.4.1.2Display the word mapDisplay the reaction diagram Show all sequences 6.4.1.2purified wild-type enzyme and mutant enzymes, free or in complex with inhibitors haloxyfop or diclofop, 10 mg/ml protein with reservoir solution containing 0.1 M sodium citrate, pH 5.5, 0.2 M NaCl, 8% w/v PEG 8000, and 10% v/v glycerol, complexing by soaking of crystals in 5 mM inhibitor solution, cryoprotection by 25% v/v ethylene glycol, X-ray diffraction structure determination and analysis at 2.5-2.8 A resolution
Show all pathways known for 6.4.1.2Display the word mapDisplay the reaction diagram Show all sequences 6.4.1.2structure of the full-length, 500 kD holoenzyme dimer. The central region contains five domains and is important for positioning the biotin carboxylase and carboxyltransferase domains for catalysis. The structure reveals a dimer of the biotin carboxylase domain
Results 1 - 10 of 11 > >>