Allostery at a protein-protein interface harboring an intermolecular dynamic network
Motional properties of individual amino acids in proteins are strongly modulated by their specific surrounding. The dynamics of tightly interacting residues can form intramolecular dynamic networks, which influence various features of protein function and serve as an access point for their modulation within signaling cascades. However, the possible formation of intermolecular networks shared between natural or constructed interaction partners has escaped thorough experimental assessment. Here, using fast-MAS solid-state NMR spectroscopy, we contrast the absence of a cross-talk between different residues in an apo protein with a recoupling of s timescale dynamics effective via a mediating crystal-crystal contact. The data show that dynamic allostery is not necessarily restricted to motionally coupled elements within a single protein but can traverse molecular boundaries. Interrogation of intermolecular dynamic networks by the strategies proposed here may shed light on the mechanisms underlying allosteric modulation of protein function in biological, pharmacological, and biotechnological studies.