Crystallization (Comment) | Organism |
---|---|
the C-terminal ligase domain of selenomethioninyl-substituted MtuLigD is crystallized by vapor diffusion using a precipitant solution containing PEG-3000 and ZnCl2. Crystals belonged to the space group P3(2)21 (a = b = 57.1 A, c = 369.0 A). 2.4 A crystal structure of the ligase domain of Mycobacterium LigD, captured as the covalent ligase-AMP intermediate with a divalent metal in the active site | Mycobacterium tuberculosis |
Protein Variants | Comment | Organism |
---|---|---|
D483A | mutant protein is inert in the ligase adenylylation reaction | Mycobacterium tuberculosis |
E530A | mutant protein is inert in the ligase adenylylation reaction | Mycobacterium tuberculosis |
E613A | mutant protein is inert in the ligase adenylylation reaction | Mycobacterium tuberculosis |
K481A | mutant protein is inert in the ligase adenylylation reaction | Mycobacterium tuberculosis |
K635A | mutant is active in autoadenylylation as wild-type LigD, consistent with its retention of overall nick-joining function | Mycobacterium tuberculosis |
K637A | mutant enzyme forms about one-fourth the level of ligase-AMP compared to wild-type enzyme. Complete loss of function of overall nick ligation | Mycobacterium tuberculosis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Mycobacterium tuberculosis |
Synonyms | Comment | Organism |
---|---|---|
DNA ligase D | - |
Mycobacterium tuberculosis |
LigD | - |
Mycobacterium tuberculosis |