Structure of the LH1–RC complex from Thermochromatium tepidum at 3.0 Å

Satomi Niwa, Long-Jiang Yu, Kazuki Takeda, Yu Hirano, Tomoaki Kawakami, Zheng-Yu Wang-Otomo () and Kunio Miki ()
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Satomi Niwa: Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan
Long-Jiang Yu: Faculty of Science, Ibaraki University, Mito, Ibaraki 310-8512, Japan
Kazuki Takeda: Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan
Yu Hirano: Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan
Tomoaki Kawakami: Faculty of Science, Ibaraki University, Mito, Ibaraki 310-8512, Japan
Zheng-Yu Wang-Otomo: Faculty of Science, Ibaraki University, Mito, Ibaraki 310-8512, Japan
Kunio Miki: Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan

Nature, 2014, vol. 508, issue 7495, 228-232

Abstract: Abstract The light-harvesting core antenna (LH1) and the reaction centre (RC) of purple photosynthetic bacteria form a supramolecular complex (LH1–RC) to use sunlight energy in a highly efficient manner. Here we report the first near-atomic structure, to our knowledge, of a LH1–RC complex, namely that of a Ca2+-bound complex from Thermochromatium tepidum, which reveals detailed information on the arrangement and interactions of the protein subunits and the cofactors. The RC is surrounded by 16 heterodimers of the LH1 αβ-subunit that form a completely closed structure. The Ca2+ ions are located at the periplasmic side of LH1. Thirty-two bacteriochlorophyll and 16 spirilloxanthin molecules in the LH1 ring form an elliptical assembly. The geometries of the pigment assembly involved in the absorption characteristics of the bacteriochlorophyll in LH1 and excitation energy transfer among the pigments are reported. In addition, possible ubiquinone channels in the closed LH1 complex are proposed based on the atomic structure.

Date: 2014
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DOI: 10.1038/nature13197

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