Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli as a His-tagged fusion protein | Mycobacterium tuberculosis |
Crystallization (Comment) | Organism |
---|---|
crystal structure of the regulatory subunit of aspartate kinase from Mtb alone and in complex with threonine are determined at resolutions of 2.6 A and 2.0 A, respectively. MtbAKbeta is composed of two perpendicular non-equivalent ACT domains (aspartate kinase, chorismate mutase, and TyrA (prephenate dehydrogenase)) per monomer. Each ACT domain contains two alpha helices and four antiparallel beta strands | Mycobacterium tuberculosis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
threonine | - |
Mycobacterium tuberculosis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WPX3 | - |
- |
Mycobacterium tuberculosis H37Rv | P9WPX3 | - |
- |
Purification (Comment) | Organism |
---|---|
using Ni-NTA chromatography | Mycobacterium tuberculosis |
Subunits | Comment | Organism |
---|---|---|
homodimer | MtbAKbeta, crystal structure | Mycobacterium tuberculosis |
Synonyms | Comment | Organism |
---|---|---|
aspartate kinase | - |
Mycobacterium tuberculosis |
MtbAKbeta | - |
Mycobacterium tuberculosis |