EC Number   |
|---|
   3.2.2.22 | - |
| 3.2.2.22 | 2.8 A resolution, space group P212121, two molecules per asymmetric unit |
| 3.2.2.22 | at 1.4 A resolution. Assignment of sequence by improved X-ray sequencing. Residues Y70, Y110, E159 and R162 define the active site. Residues N77 and N84 carry N-acetylglucosamine moieties |
| 3.2.2.22 | coarse-grained latice simulation model of sequence-structure modifications of the ricin A chain protein fold. Calculation of unfolding-folding transition temperature and evaluation of a possible unfolding model |
| 3.2.2.22 | crystal structures of several E85 mutant TCS complexes with adenosine-5'-monophosphate, E85A, space group P2(1)2(1)2(1), unit cell constants a = 38.3, b = 76.7, c= 79.2 |
| 3.2.2.22 | crystallization of precursor protein and active form, at 2.4 and 2.5 A resolution, respectively. In the precursor, the inactivation region is found on the protein surface and consists of a flexible loop followed by a long alpha-helix. Presence of this region diminishes both the interaction with ribosome and cytotoxicity, but not cellular uptake. The active site of the enzyme is too small to accomodate two glutamate residues |
| 3.2.2.22 | crystals of n-TCS, space group P2(1)2(1)2(1), unit cell constants a = 3.839 nm, b = 7.652 nm, c = 7.963 nm and mutant Y70A, space group P2(1)2(1)2(1), a = 3.830, b = 7.646, c = 7.943 |
| 3.2.2.22 | determination of the coupling of tyrosine residues, presence of energy transfer from tyrosine to tryptophan residues. The molar absorption coefficient of ricin in phosphate-buffered saline is 93900 per mol and cm |
| 3.2.2.22 | dynamics calculations suggest that steric factors cause the nucleoside to bind in an orientation where the enzyme destabilizes the formation of the oxacarbeniumion and thus precludes catalysis |
| 3.2.2.22 | E85Q, space group P2(1)2(1)2(1), unit cell constants a = 38.0, b = 75.9, c= 78.4 |
