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. 2021 Nov 2;12:6300. doi: 10.1038/s41467-021-26561-9

Fig. 1. Structure overview of the monomeric LH1-RC complex from Rba. sphaeroides IL106.

Fig. 1

a Side view of surface representations for the LH1-RC proteins parallel to the membrane plane. b Top view of the LH1-RC proteins from the periplasmic side of the membrane. Labels indicate chain IDs, and the RC H-subunit was omitted for clarity. Color scheme: LH1-α, green; LH1-β, blue; RC-L, wheat; RC-M, cyan; RC-H, salmon; PufX, orange; protein-U, magenta. c Tilted view of the cofactor arrangement viewing from the periplasmic side. Color scheme: BChl a, red sticks; spheroidenes, yellow sticks; BPhe a, cyan sticks; UQ-10, blue sticks; PufX, transparent orange cylinder; protein-U, transparent magenta cylinder, and transparent gray cylinders for all other proteins. d Comparisons of the central Mg atom positions in the LH1 BChl a molecules from Rba. sphaeroides IL106 (red spheres) with those from Tch. tepidum (green spheres, PDB: 5Y5S), protein-W-containing Rps. palustris (cyan spheres, PDB: 6Z5S), and protein-W-deficient Rps. palustris (blue spheres, PDB: 6Z5R). The structures were superimposed by Cα carbons of the RC (L, M, H) proteins. The ribbon models represent the RC-L, -M and -H subunits (gray), PufX (orange), and protein-U (magenta) of the Rba. sphaeroides IL106.