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Journal articles

Conservation of Dynamics Associated with Biological Function in an Enzyme Superfamily

Abstract : 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.
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Contributor : Michel Courcelles Connect in order to contact the contributor
Submitted on : Thursday, August 9, 2018 - 3:42:14 PM
Last modification on : Thursday, September 2, 2021 - 8:14:03 AM

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Chitra Narayanan, David Bernard, Khushboo Bafna, Donald Gagné, Chakra Chennubhotla, et al.. Conservation of Dynamics Associated with Biological Function in an Enzyme Superfamily. Structure, Elsevier (Cell Press), 2018, 26 (3), pp.426 - 436.e3. ⟨10.1016/j.str.2018.01.015⟩. ⟨pasteur-01856081⟩



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