EC Number   |
Reference |
|---|
    2.7.7.62 | - |
644278 |
| 2.7.7.62 | the solution structure has a mixed alpha/beta fold consisting of seven beta-strands and five alpha-helices, very similar to a Rossmann fold. Titration of apo-CobY with GTP results in large changes in amide proton chemical shifts. The CobY:GTP complex is unstable over time, GTP hydrolyzes and the protein converts slowly to a species with an NMR spectrum similar to that of apo-CobY. The variant CobYG153D, yields NMR spectra similar to those of wild-type CobY in both its apo-state and in complex with GTP. The CobYG153D:GTP complex is also unstable over time |
739433 |
| 2.7.7.62 | three-dimensional crystal structure of the guanylyltransferase (CobY) enzyme (mutant G153D) from Methanocaldococcus jannaschii (MjCobY)1 in complex with GTP at 2.8 A resolution is reported |
724319 |
| 2.7.7.62 | X-ray crystal structure determined by molecular replacement to 2.2 A resolution, crystals grown by the batch method, cocrystallized with GTP and diphosphate, crystals belong to space group P2(1)2(1)2(1) with unit cell dimensions a : 58.4 A, b : 87.8 A, and c : 101.6 A |
644437 |
| 2.7.7.62 | X-ray structure determined to 2.3 A resolution, crystals grown by microbatch, enzyme is crystallized in space group C222(1) with unit cell dimensions of a : 96.4 A, b : 114.4 A, and c : 106.7 A |
644436 |
