Structure of Nitrilotriacetate Monooxygenase Component B from Mycobacterium thermoresistibile
Author Information
Author(s): Zhang Y., Edwards T. E., Begley D. W., Abramov A., Thompkins K. B., Ferrell M., Guo W. J., Phan I., Olsen C., Napuli A., Sankaran B., Stacy R., Van Voorhis W. C., Stewart L. J., Myler P. J.
Primary Institution: Seattle Structural Genomics Centre for Infectious Disease (SSGCID)
Conclusion
The study presents the 1.6 Å resolution crystal structure of nitrilotriacetate monooxygenase component B, revealing a conserved C-terminal tail that may influence its activity.
Supporting Evidence
- The crystal structure reveals a homodimer with a split-barrel motif typical of flavin reductases.
- NTA-MoB contains a highly conserved C-terminal tail that may modulate its activity.
- This is one of the first crystal structures determined from Mycobacterium thermoresistibile.
Takeaway
Scientists studied a protein from a type of bacteria that helps it use certain chemicals for energy. They found out how this protein is built, which might help us understand how the bacteria survive.
Methodology
The protein was expressed, purified, and crystallized, and its structure was determined using X-ray crystallography.
Digital Object Identifier (DOI)
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