Journal
PROTEIN SCIENCE
Volume 15, Issue 4, Pages 672-683Publisher
WILEY
DOI: 10.1110/ps.051852306
Keywords
protein kinase A (PKA); phosphorylation of Thr 197; molecular dynamics; QM/MM calculations; collective motion
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Phosphorylation mediates the function of many proteins and enzymes. In the catalytic subunit of cAMP-dependent protein kinase, phosphorylation of Thr 197 in the activation loop strongly influences its catalytic activity. In order to provide theoretical understanding about this important regulatory process, classical molecular dynamics simulations and ab initio QM/MM calculations have been carried out on the wild-type PKA-Mg-2 ATP-substrate complex and its dephosphorylated mutant, T197A. It was found that pThr 197 not only facilitates the phosphoryl transfer reaction by stabilizing the transition state through electrostatic interactions but also strongly affects its essential protein dynamics as well as the active site conformation.
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