Molecular Dynamics Simulations of the Bacterial UraA H+-Uracil Symporter in Lipid Bilayers Reveal a Closed State and a Selective Interaction with Cardiolipin
Fig. 6
A. Alignment of the core domain of the final snapshot of one of the atomistic simulations (UraA-AT) with the core domain of the crystal structure. B. Ribbon structure of UraA showing the location of the bound uracil (green) and NG detergent (orange). C,D. Pore lining surfaces of the proteins aligned in A. Red is used when the pore radius is lower than 1.15 Å, green when the pore radius is between 1.15 and 2.3 Å and blue when the pore radius is larger than 2.3 Å. Note the loss of water cavity (blue) from the inward-facing passage during the simulation to produce a closed conformational state of UraA.