EC Number   |
|---|
   3.1.26.11 | - |
| 3.1.26.11 | cocrystallization with tRNAThr |
| 3.1.26.11 | crystal structure of different tRNase Z enzymes with regard to canonical sequence motifs reviewed, overview about substrate recognition and cleavage sites of tRNase Z given |
| 3.1.26.11 | each monomer exhibits the typical metallo-beta-lactamase fold, 2 Zn2+ ions are complexed at the active site |
| 3.1.26.11 | four-layer alpha-beta/beta-alpha sandwich fold determined |
| 3.1.26.11 | sitting drop vapor diffusion method at 18°C, 3.1 A crystal structure |
| 3.1.26.11 | structural features of tRNase Z summarized, overview |
| 3.1.26.11 | structural features summarized |
| 3.1.26.11 | structure of flexible arm and the zinc-bound active site determined, 1.97 A resolution, hanging-drop procedure, data collection and refinement statistics shown, flexible arm distinct from other bacterial enzymes, differences in dimer orientation probably due to unique cleavage-site specificity |
| 3.1.26.11 | structures of free and RNA-bound prokaryotic tRNase Z proteins compared, overview, electrostatic surface representation, catalytic site and cleavage mechanism indicated, overview |
