8YEE

Cryo-EM structure of in vitro reconstituted Light-harvesting complex II trimer

これはPDB形式変換不可エントリーです。

8YEE の概要

• エントリーDOI: 10.2210/pdb8yee/pdb
• EMDBエントリー: 39192
• 分子名称: Chlorophyll a-b binding protein, chloroplastic, CHLOROPHYLL B, CHLOROPHYLL A, ... (7 entities in total)
• 機能のキーワード: complex, light-harvesting, membrane protein, photosynthesis
• 由来する生物種: Spinacia oleracea (spinach)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 118529.81

構造登録者

Seki, S.,Miyata, T.,Tanaka, H.,Namba, K.,Kurisu, G.,Fujii, R. (登録日: 2024-02-22, 公開日: 2024-11-20, 最終更新日: 2024-12-11)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (2.37 Å)