6ERI

Structure of the chloroplast ribosome with chl-RRF and hibernation-promoting factor

これはPDB形式変換不可エントリーです。

6ERI の概要

• エントリーDOI: 10.2210/pdb6eri/pdb
• EMDBエントリー: 3941 3942 3943
• 分子名称: 23S ribosomal RNA, 50S ribosomal protein L14, chloroplastic, 50S ribosomal protein L15, chloroplastic, ... (59 entities in total)
• 機能のキーワード: chloroplast, translation, ribosome
• 由来する生物種: Spinacia oleracea; 詳細
• 細胞内の位置: Plastid, chloroplast : P09596 P22798 P17353 P82194 P82195 P82413 P28803 P24613 P09594 Q9LWB5 P27683 P82190 P82245 P82248 P82249 P28804 P28805 P82244 P23326 P12230 P06509 P82411 P27684 P08242 P09595 P13788 Q9ST69 P82403 P82191 P82129 P09597 P82278 P82162 P06506 P62128 P82163 P06507 Q9M3I4 P28807 O49937 P82137 Q9M3K7 P06508 P82130 P82024 P47910 P82192 P82193 P82180 P12629; Plastid, chloroplast stroma: P82231 P19954
• タンパク質・核酸の鎖数: 57
• 化学式量合計: 2196495.25

構造登録者

Perez Borema, A.,Aibara, S.,Paul, B.,Tobiasson, V.,Kimanius, D.,Forsberg, B.O.,Wallden, K.,Lindahl, E.,Amunts, A. (登録日: 2017-10-18, 公開日: 2018-04-18, 最終更新日: 2024-11-13)

主引用文献

Boerema, A.P.,Aibara, S.,Paul, B.,Tobiasson, V.,Kimanius, D.,Forsberg, B.O.,Wallden, K.,Lindahl, E.,Amunts, A.
Structure of the chloroplast ribosome with chl-RRF and hibernation-promoting factor.
Nat Plants, 4:212-217, 2018

PubMed Abstract: Oxygenic photosynthesis produces oxygen and builds a variety of organic compounds, changing the chemistry of the air, the sea and fuelling the food chain on our planet. The photochemical reactions underpinning this process in plants take place in the chloroplast. Chloroplasts evolved ~1.2 billion years ago from an engulfed primordial diazotrophic cyanobacterium, and chlororibosomes are responsible for synthesis of the core proteins driving photochemical reactions. Chlororibosomal activity is spatiotemporally coupled to the synthesis and incorporation of functionally essential co-factors, implying the presence of chloroplast-specific regulatory mechanisms and structural adaptation of the chlororibosome. Despite recent structural information, some of these aspects remained elusive. To provide new insights into the structural specialities and evolution, we report a comprehensive analysis of the 2.9-3.1 Å resolution electron cryo-microscopy structure of the spinach chlororibosome in complex with its recycling factor and hibernation-promoting factor. The model reveals a prominent channel extending from the exit tunnel to the chlororibosome exterior, structural re-arrangements that lead to increased surface area for translocon binding, and experimental evidence for parallel and convergent evolution of chloro- and mitoribosomes.

PubMed: 29610536
DOI: 10.1038/s41477-018-0129-6

実験手法

ELECTRON MICROSCOPY (3 Å)