NMR-based Structural Analysis of Threonylcarbamoyl-AMP Synthase and Its Substrate Interactions*

@article{Harris2015NMRbasedSA,
  title={NMR-based Structural Analysis of Threonylcarbamoyl-AMP Synthase and Its Substrate Interactions*},
  author={K. Harris and B. Bobay and K. Sarachan and A. F. Sims and Y. Bilbille and Christopher Deutsch and D. Iwata‐Reuyl and P. Agris},
  journal={The Journal of Biological Chemistry},
  year={2015},
  volume={290},
  pages={20032 - 20043}
}
Background: Threonylcarbamoyl-AMP synthase catalyzes formation of the biosynthetic intermediate of a critical tRNA modification, t6A37. Results: Structural analyses provide insight into the interaction between the substrates ATP and l-threonine and the E. coli enzyme. Conclusion: The threonylcarbamoyl-AMP synthase binds l-threonine and ATP cooperatively; l-threonine is required for positioning of ATP. Significance: Mechanistic insights into t6A37 biosynthesis provide an understanding of this… Expand
Slr0006-like proteins: A TsaC/TsaC2/YciO subfamily exclusive to cyanobacteria.

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