Setting the chaperonin timer: the effects of K+ and substrate protein on ATP hydrolysis.

@article{Grason2008SettingTC,
  title={Setting the chaperonin timer: the effects of K+ and substrate protein on ATP hydrolysis.},
  author={John Peter Grason and Jennifer Suzanne Gresham and Lusiana Widjaja and Sarah Christine Wehri and George H Lorimer},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2008},
  volume={105 45},
  pages={17334-8}
}
The effects of potassium ion on the nested allostery of GroEL are due to increases in the affinity for nucleotide. Both positive allosteric transitions, TT-TR and TR-RR, occur at lower [ATP] as [K(+)] is increased. Negative cooperativity in the double-ringed system is also due to an increase in the affinity of the trans ring for the product ADP as [K(+)] is increased. Consequently, (i) rates of ATP hydrolysis are inversely proportional to [K(+)] and (ii) the residence time of GroES bound to the… CONTINUE READING
21 Citations
31 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 21 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 31 references

Allostery and GroEL: By ATP: Exploring the tenets of nested cooperativity. PhD Thesis (Univ of Maryland, College Park, MD). 17338 www.pnas.org cgi doi

  • JS Gresham
  • 2004

Similar Papers

Loading similar papers…