Studies of conformational changes of an arginine-binding protein from Thermotoga maritima in the presence and absence of ligand via molecular dynamics simulations with the coarse-grained UNRES force field.

摘要: The arginine-binding protein (ArgBP) from the hyperthermophilic eubacterium Thermotoga maritima (TmArgBP) is responsible for arginine transport through bacterial cell membrane. binds a single molecule of l-arginine, which results in conformational changes due to hinge bending. Thereby, TmArgBP acquires one two possible conformations: open (without presence ligand) and closed (in ligand). Here we report molecular dynamics study influence or absence ligand on TmArgBP, using coarse-grained UNRES force field. our studies indicate that binding promotes conformation, agrees with experimental data. However, sensitivity conformation decreases becomes more flexible increasing temperature, might be related functionality this thermophilic organism T. maritima.