EC Number   |
Reference |
|---|
    6.1.1.1 | - |
650538, 702091, 703176 |
| 6.1.1.1 | 1.95 A crystal structure of mutant DELTA424-669 of CYT-18 protein. DELTA424-669 crystals are grown by sitting-drop vapor diffusion. The crystals are in space group C2 with unit cell dimensions: a = 104.88 A, b = 73.21 A, c = 56.79 A, beta = 111.35° |
662832 |
| 6.1.1.1 | a 4.5 A co-crystal structure of the Twort orf 142-I2 group I intron ribozyme bound to splicing-active, carboxy-terminally truncated CYT-18. Structure shows that the group I intron binds across the two subunits of the homodimeric protein with a newly evolved RNA-binding surface distinct from that which binds tRNATyr. This RNA binding surface provides an extended scaffold for the phosphodiester backbone of the conserved catalytic core of the intron RNA, allowing the protein to promote the splicing of a wide variety of group I introns. The group I intron-binding surface includes three small insertions and additional structural adaptations relative to non-splicing bacterial TyrRSs, indicating a multistep adaptation for splicing function |
694339 |
| 6.1.1.1 | crystal of SeMet-substituted TyrRS is obtained by the microbatch method, using an automatic crystallization robot. The crystals are grown at 20°C in a month. The crystal of native TyrRS is obtained by hanging-drop, vapor-diffusion method. Crystals of SeMet-substituted TyrRS belong to the space group P4(3)2(1)2, with unit cell parameters a = b = 66.66 A, c = 197.48 A. Crystals of native TyrRS belong to the space group P4(3)2(1)2 with unit cell parameters a = b = 65.91 A, c = 196.17 A |
662662 |
| 6.1.1.1 | crystal structure at 2.3 A resolution |
20 |
| 6.1.1.1 | crystal structure determination by X-ray diffraction, enzyme complexed with inhibitors at 2.8 A resolution, and truncated enzyme complexed with inhibitors at 2.2 A resolution |
653786 |
| 6.1.1.1 | electron density map, X-ray structure |
3 |
| 6.1.1.1 | enzyme complexed to a tyrosyl aryl dipeptide inhibitor, structure analysis |
650572 |
| 6.1.1.1 | hanging drop vapor-diffusion method. Crystal structures of TyrRS catalytic domain, in complex with L-tyrosine and L-tyrosyladenylate analogue, 5'-O-[N-(L-tyrosyl)sulfamoyl]adenosine, are solved at 2.0 A and 2.7 A resolution |
662639 |
| 6.1.1.1 | hanging-drop vapour diffusion method. The crystals belong to the monoclinic space group P2(1) with unit-cell parameters a = 49.2 A, b = 156.5 A, c = 55.2 A, beta = 94.2 |
660625 |
