Fig. 2: Structural details of the LH1 ring. | Communications Biology

Fig. 2: Structural details of the LH1 ring.

From: Insights into the divergence of the photosynthetic LH1 complex obtained from structural analysis of the unusual photocomplexes of Roseospirillum parvum

Fig. 2

a Arrangement of cofactors in an LH1 unit. The coordinated amino acid residues with BChl a molecules are shown by sticks and labeled for clarity. The color codes of polypeptides and pigments are the same as in Fig. 1. b Hydrogen bonding site around B908 in LH1 αβ-polypeptide. Both the residues involved in hydrogen bond interaction and hydrogen bond length are labeled. c Hydrogen bonding site around B803 in LH1 αβ-polypeptide. An aromatic residue involved in hydrogen bonding with B803 is also labeled. d Comparison of BChl a molecules orientation of Rss. parvum (green) with those of Rba. sphaeroides (light pink, PDB:7PBW), Rbl. acidophilus (pale yellow, PDB:1NKZ), Phs. molischianum (blue, PDB:1LGH), Mch. purpuratum (red, PDB:6ZXA), Rfl. castenholzii (cyan, PDB:8IUG) and G. phototrophica (pale cyan, PDB:7O0U). Their αβ-polypeptides are shown by grey white cartoon and carotenoid molecules are omitted for clarity. e Side view of a surface representation showing a channel (red dashed circle) in the LH1 ring which lacks a B803 molecule. Other channels are sealed by the B803 molecules (cyan). f The quinone-exchange channel between Rss. parvum LH1 α1- and α16-polypeptides. The surface representation LH1 α1- and α16-polypeptides are colored in pale cyan and are shown by the yellow ribbon simultaneously. The residues forming this hydrophobic channel are shown by magenta sticks.

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