@article{oai:oist.repo.nii.ac.jp:00001941,
 author = {Tani, Kazutoshi and Kanno, Ryo and Makino, Yuki and Hall, Malgorzata and Takenouchi, Mizuki and Imanishi, Michie and Yu, Long-Jiang and Overmann, Jörg and Madigan, Michael T. and Kimura, Yukihiro and Mizoguchi, Akira and Humbel, Bruno M. and Wang-Otomo, Zheng-Yu},
 issue = {1},
 journal = {Nature Communications},
 month = {Oct},
 note = {The light-harvesting-reaction center complex (LH1-RC) from the purple phototrophic bacterium Thiorhodovibrio strain 970 exhibits an LH1 absorption maximum at 960nm, 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 angstrom 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 Ca2⁺-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.},
 title = {Cryo-EM structure of a Ca2⁺-bound photosynthetic LH1-RC complex containing multiple αβ-polypeptides},
 volume = {11},
 year = {2020}
}