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. 2017 Jul 11;7:5158. doi: 10.1038/s41598-017-05328-7

Figure 3.

Figure 3

Lateral pressure by MGDG stabilizes LHCII in a structure dependent manner. (a) Schematic presentation of the LHCII monomer structure with degree of stabilization by MGDG (red color gradient) derived from Fig. 2b. Stabilization comprises domains in the transmembrane (helices H1 and H3) and extra-membrane domains (N-terminus, H2 and lumenal loop) of the protein; small arrows indicate contour length positions along the LHCII polypeptide. (b) Hotspots of MGDG mediated stabilization (red) in the crystal structure of LHCII from lumenal and stromal view corresponding to the highest intensities in (a) and l C ± 1 nm of the peak centers in Fig. 2b respectively. The effect of MGDG is the strongest in the periphery of the protein. Within a trimer, the monomers are represented by the surface structure, the tertiary structure (helices H1-H5 indicated) with and without pigments; gray or white: polypeptide, dark gray: pigments. (c) Steric interplay between trimeric LHCII and MGDG. Stabilization of LHCII is accomplished as the concave-like surface structure of trimeric LHCII (emphasized with dashed lines) matches the conical shape of MGDG (red); colors (gray: polypeptide, dark gray: pigments) highlight one LHCII monomer within the trimeric assembly. Structures obtained with Chimera and PDB ID code 2BHW.