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Results 1 - 5 of 5
EC Number Crystallization (Commentary)
Show all pathways known for 2.7.4.2Display the word mapDisplay the reaction diagram Show all sequences 2.7.4.21.8 A resolution. Molecule exhibits a compact alpha/beta structure and shows a sulfate molecule tightly bound to the P-loop. This sulfate ion forms hydrogen bonds with the amino group of amino acid G21 and with the side chain of R141
Show all pathways known for 2.7.4.2Display the word mapDisplay the reaction diagram Show all sequences 2.7.4.2enzyme in a ternary complex with phosphomevalonate, AMPPNP, and Mg2+, by sitting drop method, mixing 0.002 ml of 12 mg/ml PMK in 25 mM HEPES/K+, pH 7.5, 0.25 mM phosphomevalonate, 8 mM AMPPNP, 10 mM MgCl2, with 0.002 ml of 36% w/v PEG 4000, and 100 mM MES/Na+, pH 6.0, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement with EPMR
Show all pathways known for 2.7.4.2Display the word mapDisplay the reaction diagram Show all sequences 2.7.4.2hanging-drop vapor diffusion at 20°C against a reservoir containing 100 mM HEPES pH 7.5, 800 mM NaH2PO4, 8000 mM KH2PO4 and 30 mM unbuffered ATP, crystals diffract to 2.4 A resolution
Show all pathways known for 2.7.4.2Display the word mapDisplay the reaction diagram Show all sequences 2.7.4.2NMR-based dynamics and chemical shift experiments of enzyme in complex with MgADP, mevalonate 5-phosphate and the ternary complex. Binding of mevalonate 5-phosphate causes the protein to compress, whereas subsequent binding of MgADP opens the structure. Mevalonate 5-phosphate causes movement around a hinge region to permit domain closure. Amino acids H55 and R93 may act as hinge residues, D163 may be a hinge residue for the lid region. Binding of ATP or ADP causes similar conformational changes. The first nine residues of the N-terminus are highly disordered
Show all pathways known for 2.7.4.2Display the word mapDisplay the reaction diagram Show all sequences 2.7.4.2purified recombinant His6-tagged enzyme, mixing of 0.002 ml of 10 mg/mL protein in 100 mM (NH4)2SO4, 20 mM HEPES, pH 7.6, with 0.002 ml reservoir solution containing 15% v/v pentaerythritol ethoxylate, 100 mM HEPES, pH 7.6, 15% v/v MPD, 15°C, 2-3 days, X-ray diffraction structure determination and analysis at 1.76 A resolution, SAD method
Results 1 - 5 of 5