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7C9R

STRUCTURE OF PHOTOSYNTHETIC LH1-RC SUPER-COMPLEX OF THIORHODOVIBRIO STRAIN 970

7C9R の概要
エントリーDOI10.2210/pdb7c9r/pdb
EMDBエントリー30314
分子名称Photosynthetic reaction center cytochrome c subunit, Alpha subunit 2 of light-harvesting 1 complex, PROTOPORPHYRIN IX CONTAINING FE, ... (24 entities in total)
機能のキーワードlh1-rc, photosynthesis, purple bacteria
由来する生物種Thiorhodovibrio sp. 970
詳細
タンパク質・核酸の鎖数36
化学式量合計442274.37
構造登録者
主引用文献Tani, K.,Kanno, R.,Makino, Y.,Hall, M.,Takenouchi, M.,Imanishi, M.,Yu, L.J.,Overmann, J.,Madigan, M.T.,Kimura, Y.,Mizoguchi, A.,Humbel, B.M.,Wang-Otomo, Z.Y.
Cryo-EM structure of a Ca 2+ -bound photosynthetic LH1-RC complex containing multiple alpha beta-polypeptides.
Nat Commun, 11:4955-4955, 2020
Cited by
PubMed Abstract: The light-harvesting-reaction center complex (LH1-RC) from the purple phototrophic bacterium Thiorhodovibrio strain 970 exhibits an LH1 absorption maximum at 960 nm, the most red-shifted absorption for any bacteriochlorophyll (BChl) a-containing species. Here we present a cryo-EM structure of the strain 970 LH1-RC complex at 2.82 Å resolution. The LH1 forms a closed ring structure composed of sixteen pairs of the αβ-polypeptides. Sixteen Ca ions are present in the LH1 C-terminal domain and are coordinated by residues from the αβ-polypeptides that are hydrogen-bonded to BChl a. The Ca-facilitated hydrogen-bonding network forms the structural basis of the unusual LH1 redshift. The structure also revealed the arrangement of multiple forms of α- and β-polypeptides in an individual LH1 ring. Such organization indicates a mechanism of interplay between the expression and assembly of the LH1 complex that is regulated through interactions with the RC subunits inside.
PubMed: 33009385
DOI: 10.1038/s41467-020-18748-3
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (2.82 Å)
構造検証レポート
Validation report summary of 7c9r
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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