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-Structure paper
タイトル | Cryo-EM structure of a Ca-bound photosynthetic LH1-RC complex containing multiple αβ-polypeptides. |
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ジャーナル・号・ページ | Nat Commun, Vol. 11, Issue 1, Page 4955, Year 2020 |
掲載日 | 2020年10月2日 |
![]() | Kazutoshi Tani / Ryo Kanno / Yuki Makino / Malgorzata Hall / Mizuki Takenouchi / Michie Imanishi / Long-Jiang Yu / Jörg Overmann / Michael T Madigan / Yukihiro Kimura / Akira Mizoguchi / Bruno M Humbel / Zheng-Yu Wang-Otomo / ![]() ![]() ![]() ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (単粒子) |
解像度 | 2.82 Å |
構造データ | EMDB-30314, PDB-7c9r: |
化合物 | ![]() ChemComp-HEM: ![]() ChemComp-MG: ![]() ChemComp-CA: ![]() ChemComp-DGA: ![]() ChemComp-PGV: ![]() ChemComp-BCL: ![]() ChemComp-BPH: ![]() ChemComp-UQ8: ![]() ChemComp-8K6: ![]() ChemComp-FE: ![]() ChemComp-MQ8: ![]() ChemComp-CDL: ![]() ChemComp-H4X: ![]() ChemComp-LMT: |
由来 |
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![]() | PHOTOSYNTHESIS / LH1-RC / PURPLE BACTERIA |