Stiffness of the C-terminal disordered linker affects the geometry of the active site in endoglucanase Cel8A

摘要: Cellulosomes are complex multi-enzyme machineries which efficiently degrade plant cell-wall polysaccharides. The multiple domains of the cellulosome proteins often tethered together by intrinsically disordered regions. properties and functions these linkers not well understood. In this work, we study endoglucanase Cel8A, is a relevant enzymatic component cellulosomes Clostridium thermocellum. We use both all-atom coarse-grained simulations to investigate how conformations catalytic domain Cel8A affected linker at its C terminus. find that when bound substrate, effective stiffness can influence distances between groups amino-acid residues throughout entire domain. particular, variations in lead small changes geometry active-site cleft. suggest such geometrical may have an effect on activity enzyme.