Protein dynamics of resurrected ancestral enzymes studied by crystallography.

Adaptation of organisms to environmental niches is a hallmark of evolution. One prevalent example is that of thermal adaptation, where in two descendants evolve at different temperature extremes. How dynamical changes due to adaptive mutations are allosterically propagated to the active site, to modulate activity, in different thermally adapted enzyme is not known. To address this question we analyze the properties of resurrected ancestral enzymes engaged in a thermal adaptation route we recapitulated. We will solve the crystal structure several billions-years old enzymes and we will explore their dynamical properties following X-rays data collection at various temperature. We expect describing the evolutionary-driven reorganization of contacts network that are required to conserve appropriate conformational stability and efficient functional dynamics during the early steps of an enzyme adaptive process.