EC Number |
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3.1.13.4 | crystal structure of the PARN-RNA-recognition motif domain (residues 445-540) with a bound 7-methylguanosine triphosphate nucleotide shows a remarkable conformational flexibility of the RNA-recognition motif domain, crystal structure is refined at a resolution of 2.1 A, protein folds into a three-stranded antiparallel beta-sheet that is flanked by one alpha-helix connecting beta-strands beta1 and beta2 |
3.1.13.4 | enzyme PF2046 complexed with an oligonucleotide of four thymidine nucleotides (dT4), X-ray diffraction structure determination and analysis |
3.1.13.4 | free and RNA-bound forms, 20°C, hanging-drop method |
3.1.13.4 | in silico model for catalytic mechanism and development of a 3D pharmacophore model. Residues Arg99 and Gln109 are involved in the regulation of catalysis. The natural preference of the enzyme for poly(A) is based on favorable biophysical electrostatic and hydrophobic interactions |
3.1.13.4 | Pop2p crystallized by the sitting drop vapour diffusion technique, to 1.4 A resolution by X-ray crystallography, crystals belong to the space group P212121, contains a fully conserved DEDDh active site |
3.1.13.4 | purified recombinant CNOT6L nuclease domain in complex with AMP and poly(A) DNA, hanging drop vapour diffusion method, 0.001 ml of protein solution, containing 15 mg/ml protein and 1 mM DTT, is mixed with 0.001 ml of reservoir solution and equilibrated over 300 ml reservoir solution, containing 0.1 M HEPES, pH 7.5, 1.1 M ammonium tartrate, and 0.2 M NDSB-201, at 16°C, X-ray diffraction structure determination and analysis at 1.94-2.44 A resolution |
3.1.13.4 | to 2.1 A resolution, one dimer per asymmetric unit |