Fig. 1: Overall structure of the rice Si channel Lsi1 at a resolution of 1.8 Å. | Nature Communications

Fig. 1: Overall structure of the rice Si channel Lsi1 at a resolution of 1.8 Å.

From: Structural basis for high selectivity of a rice silicon channel Lsi1

Fig. 1

a Structures and the van der Waals volumes of water, glycerol, and metalloid (Si, As) transported by aquaporin. b The overall structure of the Lsi1cryst tetramer is viewed from the extracellular side. A pseudo-C4 symmetric axis is represented by a diamond shape. c Side view of the monomeric Lsi1cryst, rainbow-colored with the N terminus in blue. The khaki bars indicate the membrane boundaries. d A close-up view of the channel region (chain C). Hydrogen bonding network (dot lines) shows interactions of the water molecules and the residues facing the channel’s pore. Key residues comprising the ar/R SF are highlighted by bold letters. Two residues (Arg78 and Ser80) in green color are from an adjacent subunit. Water molecules positioned in the channel (red) and extra/intracellular regions (pink) are shown. Water molecules in the channel are labeled in blue, and with the omit map (gray) contoured at +3.5ơ.

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