Globally correlated conformational entropy underlies positive and negative cooperativity in a kinase’s enzymatic cycle

Yingjie Wang; Manu V.S.; Jonggul Kim; Geoffrey Li; Lalima G. Ahuja; Philip Aoto; Susan S. Taylor; Gianluigi Veglia

doi:10.1038/s41467-019-08655-7

Nature Communications (Feb 2019)

Globally correlated conformational entropy underlies positive and negative cooperativity in a kinase’s enzymatic cycle

Yingjie Wang,
Manu V.S.,
Jonggul Kim,
Geoffrey Li,
Lalima G. Ahuja,
Philip Aoto,
Susan S. Taylor,
Gianluigi Veglia

Affiliations

Yingjie Wang: Department of Chemistry, University of Minnesota
Manu V.S.: Biochemistry, Molecular Biology, and Biophysics, University of Minnesota
Jonggul Kim: Department of Chemistry, University of Minnesota
Geoffrey Li: Department of Chemistry, University of Minnesota
Lalima G. Ahuja: Department of Chemistry and Biochemistry, and Pharmacology University of California at San Diego
Philip Aoto: Department of Chemistry and Biochemistry, and Pharmacology University of California at San Diego
Susan S. Taylor: Department of Chemistry and Biochemistry, and Pharmacology University of California at San Diego
Gianluigi Veglia: Department of Chemistry, University of Minnesota

DOI: https://doi.org/10.1038/s41467-019-08655-7
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 11

Abstract

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Allosteric interactions are an important contributor to the catalytic properties of enzyme. Here the authors demonstrate—using the prototypical protein kinase PKA—that the allosteric cooperativity underscoring substrate recognition and product release are directly linked to changes in conformational entropy.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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