Editor's Summary

19 November 2009

Allostery goes dynamic


Effector molecules are thought to control the activity of allosteric proteins by binding to an allosteric site, distinct from the active site, thereby inducing and stabilizing a specific conformational state of the protein. A new study suggests that the notion of purely structurally regulated activity in allosteric proteins should be revised to include a frequently dominating contribution from protein dynamics. Shiou-Ru Tzeng and Charalampos Kalodimos characterized cyclic AMP binding to catabolite activator protein (CAP), a transcriptional activator often used as a model for allostery. They find, surprisingly, that even when in a structurally inactive conformation, CAP can be activated for ligand (DNA) binding by changes in protein dynamics.

LetterDynamic activation of an allosteric regulatory protein

Shiou-Ru Tzeng & Charalampos G. Kalodimos

doi:10.1038/nature08560