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EC Number Crystallization (Commentary)
Show all pathways known for 4.6.1.1Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.1-
Show all pathways known for 4.6.1.1Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.12.8 A and 2.9 A resolutions, crystal structures of the complex between stimulatory G protein alpha subunits guanosine 5'-(gamma-thio)triphosphate and the catalytic C1 and C2 domains from type V and type II adenylate cyclase, bound to forskolin and either 2'(3')-O-(N-methylanthraniloyl)-guanosine 5' triphosphate Mg2+ or 2'(3')-O-(N-methylanthraniloyl)-guanosine 5' triphosphate Mn2+
Show all pathways known for 4.6.1.1Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.13.2 A resolution
Show all pathways known for 4.6.1.1Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.13.3 A resolution active form of the catalytic domain Rv1264, 2.3 A resolution inhibited form
Show all pathways known for 4.6.1.1Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.1at 1.9 A resolution, crystals belong to space group P212121, eight highly conserved ionic residues, E10, E12, K14, R63, K76, K111, D126, and E136 lie in the barrel core and form the likely binding sites for substrate and divalent cations. A phosphate ion bound to R63, K76, K111, and R113 near the center of the conserved cluster. AC-IV active site is relatively enriched in glutamate and features an ExE motif as its most conserved element
Show all pathways known for 4.6.1.1Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.1by the hanging-drop, vapour-diffusion method at 18°C, to 1.6 A resolution, crystal structure of the histidine-tagged auto-inhibitory domain Rv1264N shows the protein in a tight, disk-shaped dimer, formed around a helical bundle, and involving a protein chain crossover
Show all pathways known for 4.6.1.1Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.1by vapour diffusion-hanging drop method, amino-terminal His-tagged construct, from which the tag was removed by thrombin, crystallized in a triclinic form diffracting to 1.9 A resolution, with one dimer per asymmetric unit and unit-cell parameters a = 33.5, b = 35.5, c = 71.8 A, alpha = 88.7, beta = 82.5, gamma = 65.5°. Non-His tagged native construct crystallized in space group P212121 with unit-cell parameters a = 56.8, b = 118.6, c = 144.5 A, to 2.9 A resolution and probably having two dimers per asymmetric unit
Show all pathways known for 4.6.1.1Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.1complex with 2-hydroxyestradiol and alpha/beta-methylene-ATP, 20-3 A resolution
Show all pathways known for 4.6.1.1Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.1crystal structure analysis
Show all pathways known for 4.6.1.1Display the word mapDisplay the reaction diagram Show all sequences 4.6.1.1crystal structure of native soluble AC and of soluble AC in complex with the competitiv substrate analogs beta-L-2',3'-dideoxyadenosine 5'-triphiosphate and adenosine 5'-(alpha-thio)-triphosphate at 2.8-3.0 A
Results 1 - 10 of 30 > >>