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Ensemble-function relationships to evaluate catalysis in the ketosteroid isomerase oxyanion hole

Yabukarski, F.; Doukov, T.; Pinney, M.; Biel, J.; Fraser, J.; Herschlag, D.

2021-09-30 biochemistry
10.1101/2021.09.29.461692 bioRxiv
Show abstract

Following decades of insights from structure-function studies, there is now a need to progress from a static to dynamic view of enzymes. Comparison of prior cryo X-ray structures suggested that deleterious effects from ketosteroid isomerase (KSI) mutants arise from misalignment of the oxyanion hole catalytic residue, Y16. However, multi-conformer models from room temperature X-ray diffraction revealed an ensemble of Y16 conformers indistinguishable from WT for Y32F/Y57F KSI and a distinct, non-native ensemble for Y16 in Y57F KSI. Functional analyses suggested rate effects arise from weakened hydrogen bonding, due to disruption of the Y16/Y57/Y32 hydrogen bond network, and repositioning of the general base. In general, catalytic changes can be deconvoluted into effects on the probability of occupying a state (P-effects) and the reactivity of each state (k-effects). Our results underscore the need for ensemble-function analysis to decipher enzyme function and ultimately manipulate their extraordinary capabilities.

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