Effects of high hydrostatic pressure on crystallographic structure of xynalase 11 to characterize the conformations of the thumb-loop involv

Xylanases in the GH11 family exhibit a jelly-roll fold with the presence of a thumb-loop positioned above the catalytic cleft. This loop is highly mobile with three predicted distinct conformations that should play a major role in the catalytic activity. However, the detailed molecular mechanisms enabling the motion of this loop are largely unknown. Furthermore, the activity of xylanase from the extremophilic species can be enhanced by 20% under hydrostatic pressure. The dynamics in the catalytic cycle is currently characterized using HP-NMR at ambient and different high pressure. The objective of this project consists at precisely analyze the pressure-induced structural modifications using high pressure crystallography. This will allow to interpret the high pressure NMR data in more detail and to characterize the different conformation of the thumb-loop. The knowledge derived from this project should push forward the development of a more efficient enzyme to degrade the biomass.