5Y6P

Structure of the phycobilisome from the red alga Griffithsia pacifica

This is a non-PDB format compatible entry.

Summary for 5Y6P

• Entry DOI: 10.2210/pdb5y6p/pdb
• EMDB information: 6769
• Descriptor: LRC6, R-phycoerythrin alpha chain, R-phycoerythrin beta chain, ... (29 entities in total)
• Functional Keywords: phycobilisome, photosynthesis
• Biological source: Griffithsia pacifica; More
• Total number of polymer chains: 862
• Total formula weight: 18059512.00

Authors

Zhang, J.,Ma, J.F.,Liu, D.S.,Sun, S.,Sui, S.F. (deposition date: 2017-08-13, release date: 2017-11-15, Last modification date: 2025-09-17)

Primary citation

Zhang, J.,Ma, J.,Liu, D.,Qin, S.,Sun, S.,Zhao, J.,Sui, S.F.
Structure of phycobilisome from the red alga Griffithsia pacifica
Nature, 551:57-63, 2017

PubMed Abstract: Life on Earth depends on photosynthesis for its conversion of solar energy to chemical energy. Photosynthetic organisms have developed a variety of light-harvesting systems to capture sunlight. The largest light-harvesting complex is the phycobilisome (PBS), the main light-harvesting antenna in cyanobacteria and red algae. It is composed of phycobiliproteins and linker proteins but the assembly mechanisms and energy transfer pathways of the PBS are not well understood. Here we report the structure of a 16.8-megadalton PBS from a red alga at 3.5 Å resolution obtained by single-particle cryo-electron microscopy. We modelled 862 protein subunits, including 4 linkers in the core, 16 rod-core linkers and 52 rod linkers, and located a total of 2,048 chromophores. This structure reveals the mechanisms underlying specific interactions between linkers and phycobiliproteins, and the formation of linker skeletons. These results provide a firm structural basis for our understanding of complex assembly and the mechanisms of energy transfer within the PBS.

PubMed: 29045394
DOI: 10.1038/nature24278

Experimental method

ELECTRON MICROSCOPY (3.5 Å)