Kitty S. P. Yip

TL;DR: The structure determination of glutamate dehydrogenase from P. furiosus contains a striking series of ion-pair networks on the surface of the protein subunits and buried at both interdomain and intersubunit interfaces, which suggest that the formation of such extended networks may represent a major stabilizing feature associated with the adaptation of enzymes to extreme temperatures.

TL;DR: The results suggest that extensive ion-pair networks may provide a general strategy for manipulating enzyme thermostability of multisubunit enzymes, however, this study emphasizes the importance of the exact local environment of a residue in determining its effects on stability.

TL;DR: The results of this analysis indicate that the ion-pair networks become more fragmented as the temperature stability of the enzyme decreases and are consistent with a role for the involvement of such networks in the adaptation of enzymes to extreme temperatures.

TL;DR: Examination of the sequence differences suggests that enhanced packing within the buried core of the protein plays an important role in maintaining stability at extreme temperatures and may modulate the dynamics of this enzyme and contribute to increased stability.

TL;DR: The structure determination of the glutamate dehydrogenase from thehyperthermophile Pyrococcus furiosus has been completed at 2.2 A resolution and it is revealed that the hyperthermophilic enzyme contains a striking series of networks of ion-pairs which are formed by regions of the protein which contain a high density of charged residues.