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- W3107698834 abstract "Abstract Several enzymes are known to have evolved from non-catalytic proteins such as solute-binding proteins (SBPs). Although attention has been focused on how a binding site can evolve to become catalytic, an equally important question is: how do the structural dynamics of a binding protein change as it becomes an efficient enzyme? Here we performed a variety of experiments, including propargyl-DO3A-Gd(III) tagging and double electron–electron resonance (DEER) to study the rigid body protein dynamics of reconstructed evolutionary intermediates to determine how the conformational sampling of a protein changes along an evolutionary trajectory linking an arginine SBP to a cyclohexadienyl dehydratase (CDT). We observed that primitive dehydratases predominantly populate catalytically unproductive conformations that are vestiges of their ancestral SBP function. Non-productive conformational states, including a wide-open state, are frozen out of the conformational landscape via remote mutations, eventually leading to extant CDT that exclusively samples catalytically relevant compact states. These results show that remote mutations can reshape the global conformational landscape of an enzyme as a mechanism for increasing catalytic activity." @default.
- W3107698834 created "2020-12-07" @default.
- W3107698834 creator A5020065219 @default.
- W3107698834 creator A5024576724 @default.
- W3107698834 creator A5027778630 @default.
- W3107698834 creator A5029220322 @default.
- W3107698834 creator A5037822811 @default.
- W3107698834 creator A5063629719 @default.
- W3107698834 creator A5063797394 @default.
- W3107698834 creator A5063975231 @default.
- W3107698834 date "2020-11-23" @default.
- W3107698834 modified "2023-10-09" @default.
- W3107698834 title "Altered conformational sampling along an evolutionary trajectory changes the catalytic activity of an enzyme" @default.
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- W3107698834 doi "https://doi.org/10.1038/s41467-020-19695-9" @default.