Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Mycobacterium tuberculosis |
Crystallization (Comment) | Organism |
---|---|
t 2.1 A resoluion. Ddl is a dimer and consists of three discrete domains. The ligand binding cavity is at the intersection of all three domains and conjoined by several loop regions. The nucleotide and D-alanine binding pockets are flexible, requiring significant structural rearrangement of the bordering regions for entry and binding of both ATP and D-Ala molecules. D-cycloserine interacts with Ddl in a manner similar to that observed for D-Ala. Each ligand binds to two binding sites that have significant differences in affinity, with the first binding site exhibiting high affinity | Mycobacterium tuberculosis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
D-cycloserine | preferential and weak inhibition at the second, lower-affinity binding site. D-cycloserine binding is tighter at higher ATP concentrations | Mycobacterium tuberculosis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WP31 | - |
- |
Mycobacterium tuberculosis H37Rv | P9WP31 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + D-Ala + D-Ala | - |
Mycobacterium tuberculosis | ADP + phosphate + D-Ala-D-Ala | - |
? | |
ATP + D-Ala + D-Ala | - |
Mycobacterium tuberculosis H37Rv | ADP + phosphate + D-Ala-D-Ala | - |
? |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.37 | - |
pH not specified in the publication, temperature not specified in the publication | Mycobacterium tuberculosis | D-cycloserine |