Fig. 2: Interactions between the linker proteins in the formation of linker skeleton of CpcL-PBS. | Nature Communications

Fig. 2: Interactions between the linker proteins in the formation of linker skeleton of CpcL-PBS.

From: Cryo-EM and femtosecond spectroscopic studies provide mechanistic insight into the energy transfer in CpcL-phycobilisomes

Fig. 2

a Interaction of CpcC1 (magenta) with CpcL (forest green). The bottom view of CpcC1 (top panel) and the top view of CpcL (bottom panel) show the spatial distribution of the residues that are involved in the hydrophobic interactions and hydrogen-bonding. LoopC1: the loop close to β1 of CpcC1. Loop12: the loop between β1 and β2 of CpcC1. b Detailed interactions between CpcC1 (magenta) and CpcL (forest green) with the same region of CpcC2 (cyan) superimposed on CpcC1. The lower panel shows the same structures shown in the upper panel with a 180-degree rotation. c Overall interaction of the Pfam01383 (CpcD) ___domain of FNR (orange) with the Pfam00427 ___domain of CpcC2 (cyan). d The interface area of CpcC2 with the relevant residues shown. e–g Three representative areas of interactions between the CpcD ___domain of FNR and Pfam00427 of CpcC2. The distances are in angstrom.

Back to article page