Narayanan, Chitra; Bernard, David N.; Bafna, Khushboo; Choudhary, Om P; Chennubhotla, Chakra; Agarwal, Pratul K et Doucet, Nicolas . Correlating functional divergence and dynamical variations in the pancreatic-type ribonuclease superfamily In: 16e Symposium annuel de PROTEO, Mai 2016, Université Laval, Québec.
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Correlation between conformational dynamics and enzyme function has been well established for discrete enzyme systems; however, approaches for characterizing dynamical properties across diverse sequence homologs and their correlation with enzyme activity remain challenging. Members of the pancreatic-type ribonuclease (RNase) superfamily share similarities in structure and fold, but display large variations in catalytic efficiencies and dynamics, making them ideal model systems to probe the relationship between conformational motions and function. Using a combination of bioinformatics, molecular dynamics simulations and NMR approaches, we characterized the dynamical properties of over 20 diverse RNase homologs, whose three-dimensional structures have been determined using X-ray crystallography or NMR approaches, over a wide range of time-scales.Our results show that while the different RNase homologs used for the analysis share a common structural fold, the dynamical properties of these enzymes are significantly different. Clustering these RNase sequences into evolutionarily distinct sub-families showed similar dynamical properties within sub-family members and significant differences between distinct sub-families. Interestingly, sequences sharing the same biological function also display similar dynamical patterns, suggesting that biological function, among other factors, may potentially impact dynamical properties influencing sequence, structure and function
Type de document: | Document issu d'une conférence ou d'un atelier |
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Informations complémentaires: | Présentation par affiche |
Mots-clés libres: | - |
Centre: | Centre INRS-Institut Armand Frappier |
Date de dépôt: | 01 mai 2018 14:55 |
Dernière modification: | 25 nov. 2020 16:33 |
URI: | https://espace.inrs.ca/id/eprint/5801 |
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