title: Insights into the molecular basis of thermal stability from the structure determination of Pyrococcus furiosus glutamate dehydrogenase.
abstract: 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.
authors.affiliation: Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, UK.
authors.forename: D W
authors.initials: DW
authors.lastname: Rice
authors.forename: K S
authors.initials: KS
authors.lastname: Yip
authors.forename: T J
authors.initials: TJ
authors.lastname: Stillman
authors.forename: K L
authors.initials: KL
authors.lastname: Britton
authors.forename: A
authors.initials: A
authors.lastname: Fuentes
authors.forename: I
authors.initials: I
authors.lastname: Connerton
authors.forename: A
authors.initials: A
authors.lastname: Pasquo
authors.forename: R
authors.initials: R
authors.lastname: Scandura
authors.forename: P C
authors.initials: PC
authors.lastname: Engel
mesh_terms: 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
chemical_list: D005969:Glutamate Dehydrogenase