The structures of Thermoplasma volcanium phosphoribosyl pyrophosphate synthetase bound to ribose-5-phosphate and ATP analogs.

@article{Cherney2011TheSO,
  title={The structures of Thermoplasma volcanium phosphoribosyl pyrophosphate synthetase bound to ribose-5-phosphate and ATP analogs.},
  author={M. Cherney and L. Cherney and C. Garen and M. James},
  journal={Journal of molecular biology},
  year={2011},
  volume={413 4},
  pages={
          844-56
        }
}
Phosphoribosyl pyrophosphate (PRPP) synthetase catalyzes the transfer of the pyrophosphate group from ATP to ribose-5-phosphate (R5P) yielding PRPP and AMP. PRPP is an essential metabolite that plays a central role in cellular metabolism. The enzyme from a thermophilic archaeon Thermoplasma volcanium (Tv) was expressed in Escherichia coli, crystallized, and its X-ray molecular structure was determined in a complex with its substrate R5P and with substrate analogs β,γ-methylene ATP and ADP in… Expand
13 Citations
Crystal structure of recombinant phosphoribosylpyrophosphate synthetase 2 from Thermus thermophilus HB27 complexed with ADP and sulfate ions.
  • 1
  • Highly Influenced
  • PDF
Pcal_1127, a highly stable and efficient ribose-5-phosphate pyrophosphokinase from Pyrobaculum calidifontis
  • 6
...
1
2
...

References

SHOWING 1-10 OF 22 REFERENCES
Phosphoribosylpyrophosphate (PRPP)‐less mutants of Escherichia coli
  • 50
...
1
2
3
...