Insights into the molecular basis of thermal stability from the structure determination of Pyrococcus furiosus glutamate dehydrogenase.
The structure determination of the glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus has been completed at 2.2 A resolution. The structure has been compared with the glutamate dehydrogenases from the mesophiles Clostridium symbiosum, Escherichia coli and Neurospora crassa. This comparison has 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. Such regions are not found in the mesophilic enzymes and the number and extent of ion-pair formation is much more limited. The ion-pair networks are clustered at both inter domain and inter subunit interfaces and may well represent a major stabilising feature associated with the adaptation of enzymes to extreme temperatures.
Rice
D W
DW
Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, UK.
Yip
K S
KS
Stillman
T J
TJ
Britton
K L
KL
Fuentes
A
A
Connerton
I
I
Pasquo
A
A
Scandura
R
R
Engel
P C
PC
D000595:Amino Acid Sequence; D001105:Archaea / Q000201:enzymology*; D004795:Enzyme Stability; D005969:Glutamate Dehydrogenase / Q000737:chemistry*; D006358:Hot Temperature; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding
D005969:Glutamate Dehydrogenase