Insights into the molecular basis of thermal stability from the structure determination of Pyrococcus furiosus glutamate dehydrogenase
| Autor: | Roberto Scandurra, I. Connerton, David W. Rice, Paul C. Engel, A. Fuentes, A. Pasquo, Kitty S. P. Yip, Timothy J. Stillman, K.L. Britton |
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| Rok vydání: | 1996 |
| Předmět: |
chemistry.chemical_classification
Clostridium symbiosum Protein Folding Hot Temperature Protein Conformation Protein subunit Glutamate dehydrogenase Molecular Sequence Data Dehydrogenase Biology biology.organism_classification Microbiology Archaea Hyperthermophile Neurospora crassa Infectious Diseases Biochemistry chemistry Glutamate Dehydrogenase Oxidoreductase Enzyme Stability Pyrococcus furiosus Amino Acid Sequence |
| Zdroj: | FEMS microbiology reviews. 18(2-3) |
| ISSN: | 0168-6445 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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