ID 56313
フルテキストURL
著者
Yu, Long-Jiang Research Institute for Interdisciplinary Science, Graduate School of Natural Science and Technology, Okayama University
Suga, Michihiro Research Institute for Interdisciplinary Science, Graduate School of Natural Science and Technology, Okayama University
Wang-Otomo, Zheng-Yu Faculty of Science, Ibaraki University
Shen, Jian-Ren Research Institute for Interdisciplinary Science, Graduate School of Natural Science and Technology, Okayama University
抄録
Light-harvesting complex 1 (LH1) and the reaction centre (RC) form a membrane-protein supercomplex that performs the primary reactions of photosynthesis in purple photosynthetic bacteria. The structure of the LH1-RC complex can provide information on the arrangement of protein subunits and cofactors; however, so far it has been resolved only at a relatively low resolution. Here we report the crystal structure of the calcium-ion-bound LH1-RC supercomplex of Thermochromatium tepidum at a resolution of 1.9 Å. This atomic-resolution structure revealed several new features about the organization of protein subunits and cofactors. We describe the loop regions of RC in their intact states, the interaction of these loop regions with the LH1 subunits, the exchange route for the bound quinone QB with free quinone molecules, the transport of free quinones between the inside and outside of the LH1 ring structure, and the detailed calcium-ion-binding environment. This structure provides a solid basis for the detailed examination of the light reactions that occur during bacterial photosynthesis.
備考
This is an Accepted Manuscript of an article published by Springer Nature
発行日
2018-04-04
出版物タイトル
Nature
556巻
出版者
Springer Nature
開始ページ
209
終了ページ
213
ISSN
0028-0836
NCID
AA00752384
資料タイプ
学術雑誌論文
言語
English
OAI-PMH Set
岡山大学
論文のバージョン
author
PubMed ID
DOI
Web of Science KeyUT
関連URL
isVersionOf https://doi.org/10.1038/s41586-018-0002-9
過去1年のアクセス数
アクセス数 : ?
ダウンロード数 : ?

今月のアクセス数
アクセス数 : ?
ダウンロード数 : ?