EC Number |
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6.4.1.2 | - |
6.4.1.2 | carboxyl transferase domain |
6.4.1.2 | crystal 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 |
6.4.1.2 | crystal structure of humanized mutant of yeast CT (yCT-H9) in complex with a human ACC2-selective small molecule inhibitor is determined |
6.4.1.2 | crystallization of the carboxyltranferase domain CT in complex with CoA, inhibitor CP-640186, or herbicides haloxyfop or diclofop |
6.4.1.2 | enzyme 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 |
6.4.1.2 | purified 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 |
6.4.1.2 | purified 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 |
6.4.1.2 | purified 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 |
6.4.1.2 | structure 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 |