Conservation of Dynamics Associated with Biological Function in an Enzyme Superfamily.

Autor:	Narayanan C; INRS - Institut Armand-Frappier, Université du Québec, 531 Boulevard des Prairies, Laval, QC H7V 1B7, Canada., Bernard DN; INRS - Institut Armand-Frappier, Université du Québec, 531 Boulevard des Prairies, Laval, QC H7V 1B7, Canada., Bafna K; Genome Science and Technology, University of Tennessee, Knoxville, TN 37996, USA., Gagné D; INRS - Institut Armand-Frappier, Université du Québec, 531 Boulevard des Prairies, Laval, QC H7V 1B7, Canada., Chennubhotla CS; Department of Computational & Systems Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, USA., Doucet N; INRS - Institut Armand-Frappier, Université du Québec, 531 Boulevard des Prairies, Laval, QC H7V 1B7, Canada; PROTEO, the Québec Network for Research on Protein Function, Engineering, and Applications, Université Laval, 1045 Avenue de la Médecine, Québec, QC G1V 0A6, Canada; GRASP, Groupe de Recherche Axé sur la Structure des Protéines, McGill University, 3649 Promenade Sir William Osler, Montréal, QC H3G 0B1, Canada. Electronic address: nicolas.doucet@iaf.inrs.ca., Agarwal PK; Computational Biology Institute and Computer Science and Engineering Division, Oak Ridge National Laboratory, 1 Bethel Valley Road, Oak Ridge, TN 37830, USA; Department of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, TN 37996, USA. Electronic address: pratul@agarwal-lab.org.
Jazyk:	angličtina
Zdroj:	Structure (London, England : 1993) [Structure] 2018 Mar 06; Vol. 26 (3), pp. 426-436.e3. Date of Electronic Publication: 2018 Feb 22.
DOI:	10.1016/j.str.2018.01.015
Abstrakt:	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 10 5 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. (Copyright © 2018 Elsevier Ltd. All rights reserved.)
Databáze:	MEDLINE
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