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• W3089388306 abstract "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 2+ -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." @default.
• W3089388306 created "2020-10-08" @default.
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• W3089388306 date "2020-10-02" @default.
• W3089388306 modified "2023-10-06" @default.
• W3089388306 title "Cryo-EM structure of a Ca2+-bound photosynthetic LH1-RC complex containing multiple αβ-polypeptides" @default.
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• W3089388306 doi "https://doi.org/10.1038/s41467-020-18748-3" @default.
• W3089388306 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7532537" @default.
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