8Y15

Cryo-EM structure of Light-harvesting complex from Spinacia oleracea

This is a non-PDB format compatible entry.

Summary for 8Y15

• Entry DOI: 10.2210/pdb8y15/pdb
• EMDB information: 38825
• Descriptor: Chlorophyll a-b binding protein, chloroplastic, CHLOROPHYLL B, CHLOROPHYLL A, ... (8 entities in total)
• Functional Keywords: complex, light-harvesting, membrane protein, photosynthesis
• Biological source: Spinacia oleracea (spinach)
• Total number of polymer chains: 3
• Total formula weight: 116995.74

Authors

Seki, S.,Miyata, T.,Tanaka, H.,Namba, K.,Kurisu, G.,Fujii, R. (deposition date: 2024-01-23, release date: 2024-11-20, Last modification date: 2024-12-11)

Primary citation

Seki, S.,Miyata, T.,Norioka, N.,Tanaka, H.,Kurisu, G.,Namba, K.,Fujii, R.
Structure-based validation of recombinant light-harvesting complex II.
Pnas Nexus, 3:pgae405-pgae405, 2024

PubMed Abstract: Light-harvesting complex II (LHCII) captures sunlight and dissipates excess energy to drive photosynthesis. To elucidate this mechanism, the individual optical properties of pigments in the LHCII protein must be identified. In vitro reconstitution with apoproteins synthesized by and pigment-lipid mixtures from natural sources is an effective approach; however, the local environment surrounding each pigment within reconstituted LHCII (rLHCII) has only been indirectly estimated using spectroscopic and biochemical methods. Here, we used cryo-electron microscopy to determine the 3D structure of the rLHCII trimer and found that rLHCII exhibited a structure that was virtually identical to that of native LHCII, with a few exceptions: some C-terminal amino acids were not visible, likely due to aggregation of the His-tags; a carotenoid at the V1 site was not visible; and at site 614 showed mixed occupancy by both chlorophyll and molecules. Our observations confirmed the applicability of the in vitro reconstitution technique.

PubMed: 39346626
DOI: 10.1093/pnasnexus/pgae405

Experimental method

ELECTRON MICROSCOPY (2.17 Å)