Titre
Structural genomics of thermotoga maritima proteins shows that contact order is a major determinant of protein thermostability.
Type
article
Institution
Externe
Périodique
Auteur(s)
Robinson-Rechavi, M.
Auteure/Auteur
Godzik, A.
Auteure/Auteur
Liens vers les personnes
ISSN
0969-2126
Statut éditorial
Publié
Date de publication
2005
Volume
13
Numéro
6
Première page
857
Dernière page/numéro d’article
860
Langue
anglais
Résumé
Despite numerous studies, understanding the structural basis of protein stability in thermophilic organisms has remained elusive. One of the main reasons is the limited number of thermostable protein structures available for analysis, but also the difficulty in identifying relevant features to compare. Notably, an intuitive feeling of "compactness" of thermostable proteins has eluded quantification. With the unprecedented opportunity to assemble a data set for comparative analyses due to the recent advances in structural genomics, we can now revisit this issue and focus on experimentally determined structures of proteins from the hyperthermophilic bacterium Thermotoga maritima. We find that 73% of T. maritima proteins have higher contact order than their mesophilic homologs. Thus, contact order, a structural feature that was originally introduced to explain differences in folding rates of different protein families, is a significant parameter that can now be correlated with thermostability.
PID Serval
serval:BIB_88A740162689
PMID
Open Access
Oui
Date de création
2008-01-24T16:47:12.659Z
Date de création dans IRIS
2025-05-21T00:02:26Z