Contribution of electrostatic interactions, compactness and quaternary structure to protein thermostability: lessons from structural genomics of Thermotoga maritima.

Détails

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Etat: Public
Version: de l'auteur
ID Serval
serval:BIB_DE7A148B9A94
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Contribution of electrostatic interactions, compactness and quaternary structure to protein thermostability: lessons from structural genomics of Thermotoga maritima.
Périodique
Journal of Molecular Biology
Auteur(s)
Robinson-Rechavi M., Alibés A., Godzik A.
ISSN
0022-2836 (Print)
ISSN-L
0022-2836
Statut éditorial
Publié
Date de publication
2006
Peer-reviewed
Oui
Volume
356
Numéro
2
Pages
547-557
Langue
anglais
Résumé
Studies of the structural basis of protein thermostability have produced a confusing picture. Small sets of proteins have been analyzed from a variety of thermophilic species, suggesting different structural features as responsible for protein thermostability. Taking advantage of the recent advances in structural genomics, we have compiled a relatively large protein structure dataset, which was constructed very carefully and selectively; that is, the dataset contains only experimentally determined structures of proteins from one specific organism, the hyperthermophilic bacterium Thermotoga maritima, and those of close homologs from mesophilic bacteria. In contrast to the conclusions of previous studies, our analyses show that oligomerization order, hydrogen bonds, and secondary structure play minor roles in adaptation to hyperthermophily in bacteria. On the other hand, the data exhibit very significant increases in the density of salt-bridges and in compactness for proteins from T.maritima. The latter effect can be measured by contact order or solvent accessibility, and network analysis shows a specific increase in highly connected residues in this thermophile. These features account for changes in 96% of the protein pairs studied. Our results provide a clear picture of protein thermostability in one species, and a framework for future studies of thermal adaptation.
Mots-clé
Bacterial Proteins/chemistry, Bacterial Proteins/genetics, Genome, Bacterial, Models, Molecular, Protein Structure, Quaternary, Protein Structure, Tertiary, Static Electricity, Temperature, Thermotoga maritima/chemistry, Thermotoga maritima/genetics
Pubmed
Web of science
Création de la notice
24/01/2008 18:47
Dernière modification de la notice
20/08/2019 17:03
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