【7/12更新】2022年4月1日からのCiNii ArticlesのCiNii Researchへの統合について

Cryo-EM structure of a Ca2⁺-bound photosynthetic LH1-RC complex containing multiple αβ-polypeptides

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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.

source:https://www.nature.com/articles/s41467-020-18748-3

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