Dépôt numérique

Conservation of Dynamics Associated with Biological Function in an Enzyme Superfamily

Narayanan, Chitra, Bernard, David N., Bafna, Khushboo, Gagné, Donald, Chennubhotla, Chakra, Doucet, Nicolas ORCID: https://orcid.org/0000-0002-1952-9380 et Agarwal, Pratul K (2018). Conservation of Dynamics Associated with Biological Function in an Enzyme Superfamily Structure , vol. 26 , nº 3. p. 426-436. DOI: 10.1016/j.str.2018.01.015.

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Enzyme superfamily members that share common chemical and/or biological functions also share common features. While the role of structure is well characterized, the link between enzyme function and dynamics is not well understood. We present a systematic characterization of intrinsic dynamics of over 20 members of the pancreatic-type RNase superfamily, which share a common structural fold. This study is motivated by the fact that the range of chemical activity as well as molecular motions of RNase homologs spans over 105 folds. Dynamics was characterized using a combination of nuclear magnetic resonance experiments and computer simulations. Phylogenetic clustering led to the grouping of sequences into functionally distinct subfamilies. Detailed characterization of the diverse RNases showed conserved dynamical traits for enzymes within subfamilies. These results suggest that selective pressure for the conservation of dynamical behavior, among other factors, may be linked to the distinct chemical and biological functions in an enzyme superfamily.

Type de document: Article
Mots-clés libres: computer simulations; enzyme catalysis; nuclear magnetic resonance; pancreatic-type ribonucleases; protein dynamics; superfamily
Centre: Centre INRS-Institut Armand Frappier
Date de dépôt: 04 mars 2019 18:32
Dernière modification: 15 févr. 2022 15:30
URI: https://espace.inrs.ca/id/eprint/7474

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