Cryo-EM structure of a plant photosystem II supercomplex with light-harvesting protein Lhcb8 and & alpha;-tocopherol

The study presents the structure of photosystem II supercomplex from Picea abies solved by cryo-electron microscopy and describes its unique features-the presence of light-harvesting protein Lhcb8 and an & alpha;-tocopherol molecule with potential physiological function. The heart of oxygenic photosynthesis is the water-splitting photosystem II (PSII), which forms supercomplexes with a variable amount of peripheral trimeric light-harvesting complexes (LHCII). Our knowledge of the structure of green plant PSII supercomplex is based on findings obtained from several representatives of green algae and flowering plants; however, data from a non-flowering plant are currently missing. Here we report a cryo-electron microscopy structure of PSII supercomplex from spruce, a representative of non-flowering land plants, at 2.8 & ANGS; resolution. Compared with flowering plants, PSII supercomplex in spruce contains an additional Ycf12 subunit, Lhcb4 protein is replaced by Lhcb8, and trimeric LHCII is present as a homotrimer of Lhcb1. Unexpectedly, we have found & alpha;-tocopherol (& alpha;-Toc)/& alpha;-tocopherolquinone (& alpha;-TQ) at the boundary between the LHCII trimer and the inner antenna CP43. The molecule of & alpha;-Toc/& alpha;-TQ is located close to chlorophyll a614 of one of the Lhcb1 proteins and its chromanol/quinone head is exposed to the thylakoid lumen. The position of & alpha;-Toc in PSII supercomplex makes it an ideal candidate for the sensor of excessive light, as & alpha;-Toc can be oxidized to & alpha;-TQ by high-light-induced singlet oxygen at low lumenal pH. The molecule of & alpha;-TQ appears to shift slightly into the PSII supercomplex, which could trigger important structure-functional modifications in PSII supercomplex. Inspection of the previously reported cryo-electron microscopy maps of PSII supercomplexes indicates that & alpha;-Toc/& alpha;-TQ can be present at the same site also in PSII supercomplexes from flowering plants, but its identification in the previous studies has been hindered by insufficient resolution.

Automated summary

This study presents the structure of photosystem II supercomplex from Picea abies determined by cryo-electron microscopy, revealing the presence of unique features such as the light-harvesting protein Lhcb8 and α-tocopherol molecule with potential physiological function.