Structure of Mycobacterium tuberculosis glutamine synthetase in complex with a transition-state mimic provides functional insights.

@article{Krajewski2005StructureOM,
  title={Structure of Mycobacterium tuberculosis glutamine synthetase in complex with a transition-state mimic provides functional insights.},
  author={Wojciech W Krajewski and T. A. Jones and Sherry L Mowbray},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2005},
  volume={102 30},
  pages={10499-504}
}
Glutamine synthetase catalyzes the ligation of glutamate and ammonia to form glutamine, with the resulting hydrolysis of ATP. The enzyme is a central component of bacterial nitrogen metabolism and is a potential drug target. Here, we report a high-yield recombinant expression system for glutamine synthetase of Mycobacterium tuberculosis together with a simple purification. The procedure allowed the structure of a complex with a phosphorylated form of the inhibitor methionine sulfoximine… CONTINUE READING