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- W2318447415 endingPage "2730" @default.
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- W2318447415 abstract "Comparing homologous enzymes adapted to different thermal environments aids to shed light on their delicate stability/function trade-off. Protein mechanical rigidity was postulated to secure stability and high-temperature functionality of thermophilic proteins. In this work, we challenge the corresponding-state principle for a pair of homologous GTPase domains by performing extensive molecular dynamics simulations, applying conformational and kinetic clustering, as well as exploiting an enhanced sampling technique (REST2). While it was formerly shown that enhanced protein flexibility and high temperature stability can coexist in the apo hyperthermophilic variant, here we focus on the holo states of both homologues by mimicking the enzymatic turnover. We clearly show that the presence of the ligands affects the conformational landscape visited by the proteins, and that the corresponding state principle applies for some functional modes. Namely, in the hyperthermophilic species, the flexibility of the effector region ensuring long-range communication and of the P-loop modulating ligand binding are recovered only at high temperature." @default.
- W2318447415 created "2016-06-24" @default.
- W2318447415 creator A5065957921 @default.
- W2318447415 creator A5072018035 @default.
- W2318447415 creator A5072105936 @default.
- W2318447415 creator A5085034941 @default.
- W2318447415 date "2016-03-08" @default.
- W2318447415 modified "2023-10-18" @default.
- W2318447415 title "Stability and Function at High Temperature. What Makes a Thermophilic GTPase Different from Its Mesophilic Homologue" @default.
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- W2318447415 doi "https://doi.org/10.1021/acs.jpcb.6b00306" @default.
- W2318447415 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26907829" @default.
- W2318447415 hasPublicationYear "2016" @default.
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