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Literature summary extracted from

  • Akey, D.; Martins, A.; Aniukwu, J.; Glickman, M.S.; Shuman, S.; Berger, J.M.
    Crystal structure and nonhomologous end-joining function of the ligase component of Mycobacterium DNA ligase D (2006), J. Biol. Chem., 281, 13412-13423.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.5.1.1 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

EC Number Protein Variants Comment Organism
6.5.1.1 D483A mutant protein is inert in the ligase adenylylation reaction Mycobacterium tuberculosis
6.5.1.1 E530A mutant protein is inert in the ligase adenylylation reaction Mycobacterium tuberculosis
6.5.1.1 E613A mutant protein is inert in the ligase adenylylation reaction Mycobacterium tuberculosis
6.5.1.1 K481A mutant protein is inert in the ligase adenylylation reaction Mycobacterium tuberculosis
6.5.1.1 K635A mutant is active in autoadenylylation as wild-type LigD, consistent with its retention of overall nick-joining function Mycobacterium tuberculosis
6.5.1.1 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

EC Number Organism UniProt Comment Textmining
6.5.1.1 Mycobacterium tuberculosis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.5.1.1
-
 Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
6.5.1.1 DNA ligase D
-
 Mycobacterium tuberculosis
6.5.1.1 LigD
-
 Mycobacterium tuberculosis