Extended Data Fig. 10: Molecular details of the PBS.
From: Structures of a phycobilisome in light-harvesting and photoprotected states
a, Alignment of ApcE with red algae homologs (PDB:5Y6P Griffithsia pacifica, PDB:6KGX Porphyridium purpureum). RMSD is 1.9 Å, differences are circled. b, Structural models of ApcC, ApcG and CpcD. CpcD and ApcC consist of a single pf01383 domain. c, Alignment of CpcG1 with red algae homologs. Circle in CpcG1 shows C-terminal domain. CpcG1 is related to algal LRC1 linker with RMSD of 0.7 Å in the pf00427 domain. The C-terminal domain of CpcG1 has homology to LRC1a with RMSD of 0.6 Å. d, Comparison of CpcC1 and CpcC2. e–g, interaction between CpcD, CpcC2, CpcC1 and CpcG1. Interacting residues are highlighted. h, Alignment of ApcD and ApcF with red algae homologs. ApcD is related to the red algal homolog with RMSD of 0.6 Å while ApcF aligns with an RMSD of 0.6 Å with its homolog. The only major differences exist in loop regions. i, Comparison of densities of ApcG between our study and13. Reconstructions of the Synechococcus sp. strain PCC 7002 PBS and Anabaena sp. strain PCC 7120 PBS show ApcG density after map smoothening (Gaussian filter σ = 1 Å).
