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We used a hybrid fluorescence spectroscopic toolkit to monitor T4 Lysozyme(T4L) in action. By unraveling the kinetic and dynamic interplay of theconformational states, we sought to elucidate the dynamic structural biology ofT4L. In particular, by combining single-molecule and ensemble multiparameterfluorescence detection, EPR spectroscopy, mutagenesis, and FRET-positioning andscreening, we characterized three short-lived conformational states within theconformational landscape of the T4L over the ns-ms timescale. The use of 33FRET-derived distance sets, to screen known T4L structures, revealed that T4Lin solution mainly adopts the known open and closed states in exchange at 4$\mu$s. A newly found minor state, undisclosed by at present more than 500crystal structures of T4L and sampled at 230 $\mu$s, may be actively involvedin the product release step in catalysis. The presented fluorescencespectroscopic toolkit is anticipated to accelerate the development of dynamicstructural biology.

Resolving dynamics and function of transient states in single enzyme molecules