Conservation of Dynamics Associated with Biological Function in an Enzyme Superfamily

Structure
Chitra NarayananPratul K Agarwal

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.

Citations

Jan 31, 2020·Proteins·Arangasamy Yazhini, Narayanaswamy Srinivasan
Jun 28, 2018·Frontiers in Molecular Biosciences·Chitra NarayananNicolas Doucet
Oct 28, 2019·Frontiers in Pharmacology·Guillem Prats-EjarqueEster Boix
Jul 1, 2020·Science Advances·J A ByunG Melacini
Oct 15, 2020·Current Opinion in Structural Biology·Bentley WingertIvet Bahar
Dec 25, 2019·Archives of Biochemistry and Biophysics·Alejandra A CovarrubiasDavid F Rendón-Luna
Sep 17, 2020·Science Advances·J A ByunG Melacini
Apr 27, 2021·ChemCatChem·Pratul K AgarwalNicolas Doucet
Dec 7, 2018·Biochemistry·Pratul K Agarwal
Jul 18, 2018·Journal of the American Chemical Society·Stephen BoultonGiuseppe Melacini

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