Extended Data Fig. 5: Interactions between PBS and PSII.
From: In situ structure of the red algal phycobilisome–PSII–PSI–LHC megacomplex
a, Overview of LRC3, LPP1 and LPP2 interacting with both PBS and PSII from two different views. b, The interactions of LRC3 with CP43′ and PsbH. The amino acids involved in interaction are shown as sticks. c, A C-terminus shift of Psb34 occurs due to the interaction between LRC3 and Psb34. d, Electrostatic interaction of LPP1 with PBS core and PSII. e, Structural alignment of LCM and LCM′. The arrow indicates a shift of LCM-PB-loop. f, Sequence alignment of PB-loop/ LCM from different red algae and cyanobacteria. PB-loop of LCM is highlighted by a solid line. Key residues participating in interactions are marked as red triangle. Used species are red algae: Porphyridium purpureum, Griffithsia pacifica, Rhodymenia pseudopalmata and Chondrus crispus and cyanobacteria: Synechocystis sp. PCC 6803, Synechococcus sp. strain PCC 7002, Anabaena sp. PCC 7120 and Thermosynechococcus vulcanus NIES-2134. g, Overview of LCM/LCM′ and ApcD/ApcD′ interacting with PSII. h, Structural alignment of LCM and LCM′. The arrow indicates a shift of LCM-PB-loop. i, Interaction of ApcD (left), ApcD′(right) with PSII-d1 and PSII-d2. c, Structural alignment of CP43 from PSII-d1 and PSII-d2. Steric hindrance created by ApcD′ is shown as surface representation in red box. The arrow indicates the N-terminus shift of CP43/PSII-d2 due to the steric hindrance.
